BDH eae es ‘Broostons i, Bi eH Sr Learning Objectives ‘Ie earning objectives relating fo the structure and function of ete ald are proised the lone Molecular Genetics” Ct. Compile your own glossary trom the KEY WORDS ‘spayed in bokd type inthe learning objectives below, Understanding organic chemistry (page 102) 2. Listthe four most common elements found in tng thing. Provide examples of were these elamaris coeur in eal. Distinguish between an atom and an fon. Expain what's maant by organic chemistry anc ‘explain its importance in biology. 8. Distinguish between ionis bonds and covalent bonds and understand the importance of covalent bonds in carbon-based compounds. G4, Cistinuish between monomers and polymers and provide examples of each ype. Expaincleatly whats meant by a macromolecule and give examples. 15. Explain how the laws of thermodynamics relate to the biochemical processes accurring in ining systems Undersiand the concept of free energy and expain how the concapt of free energy helps to determine whether of nota process wil occur spontaneously. Explain the terms endergenic and exergonie in rebtion to thei ree energy changes. Water and inorganic ions (pages 102-103) 6. Deserbe the structure of water, intudng reference to the polar nature cf the watar molecule, the nature of the bonding wthin the molecule, and the Importance of hydrogen bonding belwean water molecules. 1D 7. Identity the prysical properties of mater that are Important in biological sysiems. Explain why water is termed tho universal solvent and describe Is various Dlologcal roles: e.g. molabolic role, asa solvent as @ lubricant, as @ coolant, as a transport medium, and as ‘2 fluid n iycrostatio skeletons and cal turer. 1D 8. Provide a defriton ofan inorganic (mineral) fon. With feterence Io specific examples, descibe the role of Inorganic ions in bloglealsysiams, Examples coud Inelude: Na’, K°, Mg, Cr, NO, and POS Carbohydrates (pages 104-105) 1B &,_ Describe the basic composition and general formula of carbohydrates, Explain the main roles of carbohydrates In both plants and arimats. 110, Deserts what is meant by a monosaccharide and ‘ve its general formula. Provide examples of triose, pentose, and hexose sugars (Including ructose and (galactose). For each, dently is biological rola The Chemistry b BeceaDerES a na ie 11, Approsiate that monosaccharides show isomerism. Recognize siuctual isomers of glucose (a and f slucase) and understand thee belogica significance. 42. Deserve what is meant by a disaccharide. Expiain how disaccharides are formed by a condensation reaction and broken apart by hydrolysis. Identify tho ‘lyeosidic bond formed ard broken in each ca Give examples of dsacchardes and ther functions, ‘and name the monosaccharides Involved in each case. 13, Explain what is meant by a polysaccharide anc ‘escrive how polysaccharides are formed. Describe the molecular structure ofthe folowing examples of polyeaccharidos: starch, glycogen, coluiase and relate {her structure to helt luneton in biological systome, Lipids (pages 108-107) a ‘Amino acids and prot o +4, Describe the general properties of lipids. Recognize the versity of lps in bitogical systems and describe their functional roles. Consider: phosphotipis, wares, steroids, and fats ad ol 46, Recognize that most Iipids are tiglycerides (tiaoy lyoeroe). Describe how trigiyoerdes are casstied as {als of ols and oxplain the basis ofthe classtiaton 16, Using a diagram, decorbe the basic stucture of a ‘rigyeerde. Explain thei formation by condensation reactions between glycerol and thee fatty acics. Ientiy the ester bonds tha resi rom this. Distinguish between saturated and unsaturated fatty ‘acids and relate this ctlerence tothe properties of the {at or of that results, 47. Using a diagram, deserbe the basic structure of a phospholipid and explain how it rs from the Siructure of a tglyoeride. Explain bow the structure of Phospholipids is important to their rol in membranes. ins (pages 108-112) 18, Draw or desoriba the general structure and formula fof an amino acid. Explain the basis forthe lillerent proper of amino aca. 18, Recognize that, of over 170 amino acies only 20 ‘are commonly found in proteins. Distinguish between ‘essential and non-essential amino acids. 20. Distinguish between polar and non-polar amino acids ‘and exalan their biologecal significance. 21. Appreciate the basis of optical isomerism in amino ‘acids, Distinguish L- and forms and idently which form active n biological systems. 22, Using a dagram, describe how amino acids are joined togetner in a condensation reaction to form ‘ipeptides and polypeptides. Describe the nature of popiide bends tha! result. Describe how polypepties {aro broken down by hydrolysisIdentity whore {inthe cell) proteins are made and recognize the ways in which they can be mociied after production, Distinguish between the primary structure fof @ protein and tis secondary structure, Recognize ‘ne two main ypes of secondary structure found in proteins: aloha-hol and B-pleated shect. Enplain wnat is meant by he tertiary structure of a protein and explain how it arises. Describe the relationship betwoon tho tertiary stucture ofa globular protein and its biological function. ‘ith reference to examples, ietnguish between ‘lobular and fibrous proteins. Consider the structure, properties, and biological functions of the protein. ‘With reference to spectc examples (e.9. collagen, Insulin, hemoglobin), deserive the role of ferent yes ‘of bonds in proteins: hydrogen bonds, onic bonds, (ins Textbooks and Lecture Notee: » & Coo ‘vel bology rovelen uee ard others \OTECHNOLOGY > Applications in technology > Industral Biotechnology: + Aout nduetelenzymae » Chaps 18:industil ricrbllogy * Sscover enzymes and ohers CELL BIOLOGY AND BIOCHENISTAY:+ Co EimectlarBologyenine + Moca logy ‘eso bok... and otters Biochemistry and Metabolic Patways: » Eraymes * Eo) and onzyres + Energy enymes and eats Drblem set » Reacts and onaytnes = The Biology projet: Blachamstiy Photocopying Pei [J ® Boson ktematora 2001-2005rs we i « eR (om, > FES Veo Biological Molecules The molecules that make up living things can be grouped into five classes: water, carbohydrates, lipids, proteins, and nucleic fcids, An understanding of the structure and function of these, molecules is necessary to many branches of biology, especially biochemistry, physiology, and molecular genetics. The diagram ‘below illustrates some of the common ways in which biological molecules are portrayed. Note that the molecular formula, exoresses the number of aloms in a molecule, but does not Convey its structure; this is indicated by the structural formula, “The role of water in biological systems is described opposite. ‘The rarer next to Portraying Biological Molecules Ho Tecnboraomoee Hy ‘spd for identification —>1C ‘rotenone ‘changes shape H—C—OH i HOC—H HG — OH CohlizOs HOH Glucose WG OH 4 Molecular Structural formula. Structural forma formula’ Ghesss uae ion) a gucose ongyorm) Ball ang atlgk model ‘Space filing model "Giucose Be ‘D-glucose Biological molecules may also include lems other than carton, oxygen, and Examples of Biological Molecules Key to Symbols hydrogen atoms, Ntrogen and suRur are components of molecules such a5 @ Ccatbon amino acids and nucleotides, Some molecules contain the C=O (catbon/) Soups goin jared mnt O evs ‘ona hydrogen atom it forms an aldehyde, Hits located ebweon two ‘Acetate Formaldehyde Oysteine O onsen carbon ales forms a ketone P 7H OH p ) Yoo on @ evagen Heac Head HC-C0”H.N-C{" HSC - C-CC ‘c “oo ‘0 ‘0 Nao: © sutur Ketone Aldehyde Carboxyt te =o Water and inorganic Ions Water provides an environment in at ‘wich metabolcreacfons can Fapoen, pet fal Sugenis ‘Water takes part in, and is @ common ® tena procvt o, many raatons. Tha most behavior of water dipole nature Qs atazee ‘Rhos a onal positive charge on each ff the two hydrogens and a small negative charge on the oxygen, Wator molecule Formal: PO Inorganic tons are impoctant for the Name ‘Water surroundi a negative ion (Cl Wator surrounding a positive ton (Na) Biological role seieaeu aed mansboken erat ine Calum Component af bones and teeth trganisms. An ion is simply an atom Magnesium Component ot chioropyt (or group ot atoms) that nas gained oF Iron i) Component of hemoglobin Tet one or mae cons Many of Nuete Component of amino acids of the inorganic lons required by ene ee brganisms and thelr biological roles Sodium Involved in the transmission of nerve impulses are listed in th table on the rg. k Potassium Involved in controling plant water balance or Chloride Involved in the removal of water from urine 1. On the diagram above, showing a posite and a negative ion surrounded by water molecutes, craw the positive and negative charges on the water molecules (as shown in the example provided in the same panel). Code: AlCe A uae Gee ad {oe sess dense than water. High surface tension. Low viscosity, Liquid at room temperate Colorless wih a high tensmission of visble light. Strong cohesive properties and high tensile strenath. Many substances can dsove in water (Ris clasiied ‘as a universal solver) ‘Signifeant amounis of energy ar required before water \Wil change state (high latent heat of fusion) In order for water to evapora it must absorb a large ‘amount of energy (high latent heat of vaporization). ‘Water can absort a lot of energy for only @ smal rise Intemperature (high specif heat capaci). Froatngien provides habia for Wes ona suroas prevent Vister provides nablat for Ozeanaand urge water boles Wostorgarisme quire regular aguate plans and ana. lendio be ema sabe, Wak anima eochas seals waterless rom las Cue ose lee ost and als naites he underyng wet. Water forms droplets on sures and rns of Water tows though very sal spaces and cpiates Ligld mci fo agua an inside ote Lat penetatas tau and aquatic enronmerts Water can belted and does not pull apart easly Medium forthe chemical ceactions of ite (metabolism). \Wiateris the main ransport medlum in organisms. Contents of cols are untkely to freeze, Heat is lost by evaporation of water. Sweating and transpiration causes rapid cooing, ‘Aquatle environments are thermaly stab, (Organisms have stable intrraltemporatures whan the ‘external temperature is fluctuating, 2. Explain the importance of the dipole nature of water molecules to the chemistry of life: ks ec o paso). 3. Identify the three main elements comprising the structure of organic molecules: 4, Name two other elements that are also frequently part of organic molecules: 5. State how many covalent bonds a carbon atom can form with neighboring atoms: 6. Classify formaldehyde according fo the position of the C=O group: 7. For (aj-(e), state the property of water that is significant, and give one example of that property's biological importance: (2) Property important in clarity of seawater: Biological importance: (©) Properly important in water traveling up the xylem tissue in plants: Biological importance: (©) Property important in transport of glucose around the body: Biological importance: (@) Property important in the rolatvoly stable temperature of water bodies: Biological importance: (@) Property important in the cooling effect of evaporation: Biological importance: A ese eaten 20105 ES rca % e YsaMs. 8. Bee i ostd =. = PRT Lae x. x ° Carbohydrates Carbohycrates are a family of organic molecules mace up of ‘carbon, Fydrogen, and oxygen atoms with the general formula (CH,O},. The most common arrangements found in sugars are hexdse {6 sided) or pontase (5 sided) rings. Simple sugars, of ‘monosaccharides, may jain togother to form compound sugars: (Giseccharides and polysaccharides), releasing water in the ‘process (condensation). Compound sugars can be broken down Monosaccharides Monosaocherdas are used as pimary energy source fr hekng ca metabolam. They ara singie-sugar motocules and include glucose (arapo sugar and blood suger) and fcose (heney ard tru juices) The commoniy aecutng monosaccharias conain botwosn thiee land seven carbon atoms fn thee carbon chains end of these the 6C hexose sugars oor mest requery. Al mmonosactharides are classed fs reducing sugars (Lo. hey can partoipateinreducton reacons) Single sugers (monosaccharides) ‘Those a 2 9.10080, 29. ucose, eg-gloereidehyto — deoryribose Inuciose, galactose Polysaccharides Collulose: Catulose isa structural material in plans ‘and ie mado up of unbranched chains of B-glucose molecules held tagothor by 1,4 glycosidic links. As many as 10 000 glucose molecules may bo linked together fo form a straight chain. Parallel chains bbeceme eosssinked with hyerogen bonds and ferm bundias of 60-70 molecules callod microtiois, Colllose microfiore are very strong and are a major component ofthe structural components of plants, such as te cal wal (phot, ght). ‘starch: Starch is also a polymer of gluense, but tis ‘made upoflong chins of a-glucose rolecwiosinkec together. It comains a mixture of 25-30% amylose {unbranched chins ink by 0-1, 4 alyeelaio bonds) ‘and 70-75% amylopectin (oranched chains with o-t, ‘| ghcoaic bonds every 24-30 ucose units). Starch isan energy storage molecule in plants and is found ‘coneantrated ininsoluba tarch granules win plant ‘cela (280 phot righ). Starch can bo acl hykolyzed by enzymes to soluble sugars when requir. Glycogen: Glycagen, ke slarch, is a branched polysaccharide. kis chemically simisrto avylopectin, being composed of o-glucese molecules, but there fare more o-18 alycosici inks mined with 0-14 inks, ‘This makes fore highly branched and water-soluble shan stareh, yengan is storage compound in animal tiseues andi found mainyin ver and muscle cols {photo right). hie eadily hydrolyzed by onaymes to form glucose, Chitin; Chitin is 2 tough moditiod poh ‘mado up of chaine of glucose mol chemically similar to colulase but each glucose has fan amine group (-NH2) attaches. After collulose, coin isthe escond most abundant cerbohycrato. It Js found in the cell walls of fung! and ls the main ‘component af the exeskeloton of nsec (right) and Code: A2 into theit constituent monosaccharides by the opposite reaction {hydrolysis}. Sugars play a central role in coll, providing energy ‘and, in some calls, contributing to support. They are the major ‘component of most plants (60-90% of the dry weight) and are used by humans as a cheap food source, and a source of fuel, housing, and clothing, In all carbohyorates, the structure is closely related to their functional properties (below). Disaccharides Diesocharides are double-sugar molooul and are used as enecay sources and as buiding blocks for larger molecules. The ype of ‘sacchari formed dapands on the meromors invived and whether they aren there or fi term. Only afer csaccnaries (e.g actose) fe assiied as reducing sugars, ‘Sucrose = o-glucose + fructose (mpl sugar found in pant sap) Naltoee = ecguoose + a-iucoge (a prosuet of starch Ryeolsis) Lactose = f-ghucoae = B-gatctose (rik sugar] Cellobiose = flucose + f-lucoso (kom collie hycoyss) ‘Double sugars (isaccharides) Examples lactose, rmalose, calobiose Bread ry ecard pemee) ponents] Peas Se pi Photocopying ProhibitedIsomeian Cnpeund th he same chemi mal (sane 6 wes nd rer aoe) ater the MZ tangent ft ton, Such vals the tanga or mance ee caldeone oo AN Thatiutural isomer (euch as fucose and gcse, OF oN tate wand gums eg te atone a fed Storr coor, Opal ome ae orl how hoon every voy rome nage o enc aber See outs cHOH I onsen tan smnbne sm coe syn ono exo that scald a endenstonreacten Compound supts can Be rckan coun ey hyarlyse to simp mononaecharse, \ Js A ee ge OH H ‘ ‘OH 4 ‘\ o- = 2. Condensation reaction Hydrolysis reaction 4 on 4 on “wo monosaoznces whona dsceshard nent ax glucose «glucose Jsiaa egotor to form a | | asinto peer aren Gesecmrde win morose |_| S-mtermolsle ates se > H0 at wsicemaleas trons | | s sou of myiogon and israrey crey'ssupstes | | tyros op. Te acon by a nuiot sugar (eg. | | t calayzod by enzymes. oHoH wtatoso OH ADP glucose). 7 Disacoarge <> \ Le A mK A) f A Np NN VS yo Shee one on eae # 1. Distinguish between structural and optical isomers in carbohydrates, describing examples of each: 2. Explain how the isomorie structure of a carbohydrate may alfect its chemical behavior: 3. Explain briefly how compound sugars are formed and broken down: 4, Discuss the structural differences between the polysaccharides cellulose, starch, and glycogen, explaining how the differences in structure contribute to the functional properties of the molecule: Photocopying Prohibited a re *, reo re ery Anz Fak, vy te disks 2 ak a eles yi eo iE » ‘ *Lipids ~ Pie pes are a group of organic compounds wth an oly, greasy, serve as stuciral components in plasma membranes, Potens 7 of waxy consistency. Tey are relatively Ingouble In wator and and earoonycrates may be converted info fats by enzymes anc tend to be water-repeliing (e.9. cuticle on leaf surfaces). Lipids stored within cells of adipose tissue, During times of plenty, this . pling (2. 8 el ‘bec, 8 Important ological fuels, some are hormones, and some store is increased, to be used during times of food shortage. i i Neutral Fats and Oils zB “The most ebundant pis inning things are neutral ae fate They make up the ats nd os ound plants and animals. Fats are an economical way to store fol reserves, since they yield moro than twice 2s ‘much energy asthe game quantly of earbohyarat. wy | Mostarese comm orasbeert ase : tacts oe (rome) to ee) i ‘or three (trighceride) fatty acids. The fatty acid chains Fatty aod wz, | moyeosoun or uated ea on, Wares ‘ Seamer swawetos sodas heya Tigyetd:en exams areal et P ‘Sut win comb seared! ge be « Condensation reactions “ ‘Throe soparate condensation reactions: i 7 Tonsicsnecncrgatarets iy oly eucocenpen cee iT | Coie ayeolestomnnendyeers TPOTH Heo ee wpe aercAe os we if bonds with three fatty acids. Glycerclis w-G-o-W O-CO-CH- CH, = | HC —O-CO- CHP oH, oR OH f fan alcohol containing three carbons, i i ©. | Hickeiiewcatabutoomdion set-onn onconcyeey wbmocomcir en, oH 7 hydrox COM) group. When gyeeral ‘ # ond ey a8 on enereord “ahi is formed and water is released. Glycerol + ~——Fatty acids Tigyocrido = Water ~ ae ss Saturated and Unsaturated Fatty Acids - Pimitic acd (saturated fatty acid) Fatty acide aro a major component of neutral tats and ‘Dhospholipide, About 90 aliferent kinés are found in animal piss, Saturated faty acide contain tho maximum eumber of hydrogen atoms, Unsaturated fatty elds conan ome carbon ‘atoms that are double bonded wth each other end are rot uly Salurated wih hydrogens. Lipids containing a high proportion Linolete acid (unsaturated faty acc) of salurate fatty acs tnd to be solids at room temporature (@.g butte. Lipids wth a nigh proporton of unseturated ay acids are ols and fond to be lquid at room temperature Fogartlss of thelr dogre0 of saturation, fay acids yo large mount of energy won oxicized Phospholipids Phospholipids are the main component of celular membranes. “They consist of a glycerol attached to two fatty acd chains ‘and a phosphate (PO,?) group. The phosphate end of the moleovie i attracted to water (tis hysrophise) while the fatty ci ends repelled (hydrophobic. The hydrophobic ands turn inwards in the membrane to form a phospholipid bilayer. Hyseophoti ond Fay ace | { Faty ade Phospholipid Hydopati one Steroids [though storoids are classified as lipids, thor structure is quite iferont rom tht of other linids. Steroids have @ basic sttucture of three rings made of 6 carbon atoms each end a fourth ring containing 5 carbon atoms. Examples of sterols Include the mato and female sex hormones (testosterone and estrogen}, and the hormones cortisol and aldosterone. Cholestorol, while nota steroid ite, is sterllipic and is 2 procutsor to several steroid hormones. C9 cee curseWaxes and olls secreted on to surtaoas rovde waterproofing plants and animals of cotular membranes, Foatabsotbe checks. Orne tat are prone ta bumpe and shooks (09. kidneys) respiration stored Hpids are metabolized for ‘cuchcned wit aralavely ik yor oft. energy, producing water er carbon oxida, 1. Outline the key chemical difference between a phospholipid and a triglyceride: 2, Name the type of fatty acids found in lipids that form the following at room temperature: (@) Solid fats: (0) Ols: 3, Rolate the structure of phospholipids to their chemical properties and their functional role in cellular membranes: 4, (@) Distinguish between saturated and unsaturated fatty acids: (©) Explain how the type of fatly acid present in a neutral fat or phospholipid is related to that molecule's propertios: (6) Suggest how the cell membrano structure of an Arctic fish might difer rom that of tropical fish species: 5. Describe two examples of steroids. For each example, describe its physiological tunctin: (a) wo) 6. Explain how fate can provide an animat with: (a) Energy: (0) Water: {) Insulation: Photocopying Prohibited la pag? = Fy 3 fal g Fa 3 I Ey é Spek, AA CUP LE ee YH Ve “ey eat ok A A akV inks. Dae vi + x&Amino Acids * % [Amino acids are the basic units from which proteins are made, from their dat, All other amino acids can be constructed from ' Plants ean manufacture all the amino acids thay require from these essential amino acids. The order in which the different —_gimpler molecules, but animals must obtain a certain number amino acids are linked together to form proteins is controled le. _of ready-made amino acids (called essential amino acids) by genes on the chromosomes. ‘ne #7 group vos a Structure of Amino Acids EET, General structure of ‘hore are over 180 amino acids fund Suenype tina td ‘an amino acid ‘rel, but only 20 oocureommony in proteins, The remaining, non-eretein ceton [nino acid have specialized ols as aon OR : fe ‘romednes cots teacone-et \ Rig te nurtiansmiters an hormones: Al Aine a wy fee socsnave aconmen sre geo COOH} NHzC-C¢ be (see ig Tha only atarence betwean t HOH pa tho afore types te with tha gro tegen — Earle o en ama oh : in the goneral formu. This gfOUD IS " Ccartoe gop soounasa space tg - ‘variablo, which means that itis diferent rakes tre moleosie modet cystoin. F in each kin of anino 2 eave he ek ct. * ~*~ Propertios of Amino Acids The'Rt geupcantom —THe'R goup ghee “Ti group ges La ‘Three examples of amino acids win saftdebrdgea vin heamno sod sn — NH ¥ Siferet chemical proparies ara shown GrarGfaceresmrestealsingoreny Gi, | 4 fight wit their spect" oroups palpate can cH, ip catined, To" groupecantavequie sH cH, codon a hereechomca properee. on, i cH, sy wi}@Q-{coon) [nw.}-{coon) (nH,}+@-{coon) f C we w H w we cysteine Lysine Aspartic acid ae 7 iB ! ‘Apolypeptid chain “The cider al emin ain a preen | | ssirestad by he order of wr i ot tucletes m DNA and MANA 3 I ats: ofa Me. | Peptide bonds Sik amino acids fe 7 es - : at i oh togotberin eng poymars eo oe ge Se Ter er parte rae ese ay om ~ — * — ey w [Amine acide occurring In proteins 2 ‘The amino acids are linked together by peptide bonds to form long Alanine ycne Srna chai of up o several hundred amino acs (called palpepie chars). anina inctarets fe-etsaana 2 “Those chine may b furconal nts (compte by hemscives) they Nene entre @ —Tiorine ® i ray need tobe Jone to ater polypeptide chains before they can carry eS tuttheirfunclon Inhumere, otah amino acts can be manufactured «ASPawicacki Leucine # Tryptophan = by ourbody: ten mustbe taken In wth our ie (eight in adits). These Oveine Deena cee oe, azote eesonin amino aces (dead byte symel ontheron), Stamina Malone | Ylne @ a lead enyllanino WS 1. Describe the biological functions of amino acids: ——__ uo 8 VIG EOS, x7, Ms Describe what makes each of the 20 amino acids found in proteins unique: —_____ Photocopying ProhibitedOptical Isomers of Amino Acids All amino acts, apart from the simplest ‘ono (gine) chow optical isomerism. The two forms thet these optical isomers can yi / take relate to the arrangement othe four cf chy bonding stes on the carbon atom. This LENIN fee NGA ‘ean resut in two diferent arrangements RAN Nee NY as chown on the diagrams on the right aif a Witha very few minor exceptions only the Cartons ietahodal forms are found in ving organisms Bonding arangomont Donne forme COOH COOH ° " Condensation and Hydrolysis Reactions called a condensation reaction, Peptide chains ean be broken HO br YO HL p ets cna oes WW My bho? CI zane CI fit ete Mette Contnsaon acon | | nose enten “Two amino acids are joined |_| When « dipeptide is epi, ean - > HO totermadiperioo wih te | | ee cere inte proves of Condensation | | Hyco Mumeetatmees | | Sate warren von rion some pen Cd nH LO BR lo G COO Pe Gren rc Denice . X\ 5 Wee HOH Ho + wate eee Dipeptide 8. Deseribe the process that determines the sequence in which amino acids are linked together to form polypeptide chains: 4. Explain what is meant by essential amino acids: 5. Deseribe briefly the process of the condensation reaction for amino acids: 6. Describe briefly the process of the hydrolysis reaction for amino acids: 7. Name the optical isomeric form that occurs in neariy all amino acids in living things: fg recs roms yi x Fd fa fal g Fa 3 2 3 e uk she Soest eye. 231 ot! ny io * Las aed iste's &. +E reaBty ya a8 eon VERS ¥ Fe. ms ws TON EVI G vy BAS Teg ES TOR td Mi far Proteins The precise folding up of a protein into its tertiary structure croates a three dimensional arrangement of the active 'R' groups. ‘The way each 'A' group faces with respect to the others gives the protain its unique chemical properties. Ifa protein loses this, Primary Structure - 1° (amino acid sequence) Strings of hundreds of amino acis lnk together wilh papido bonds te frm molecules ealed polypeptide chains. Tharo are 20, “ferent kinds of amino acs that can be linked together in avast umber of clferent combinations. This sequence is called the primary structure, Its the arrangement of atiraction and repulsion points the amino aol chain that dtermines the higher levels of organization inte protein andits biological uncon, Socondary Structure - 2° (o-helix or B-pleated sheet) Polypentides become folded in various way, refered to asthe ‘socendary (2°) structure. The most common types of 2° stuctures se a cole a-hellx anca Ppleated sheet. Socondarystucures ‘are maintained witn hysrogen Bonds Detwoen neighboring CO and NH groups. H-bonds, although inividuelly weak, provide ‘considerable strongih whan thre are a large number of them, ‘The example, right, shows the two main types of secondary structure. In both the 'R side groups (not shown) project out fram the structure. Most globular protein contain regions of = holicos togethor with B-sheets. Keratin (a Rbrous protein) is composed almost entirely of erhelces. Fibro (ik protein, is ‘another fibrous protein, almost entirely in fshoot on, Tertiary Structure - 3° (foloing) vary poten hasa precise streture formed bythe foiing of the ‘eccndary structure inte @ complex shape callod the tertiary ‘structure. The prtoin folds up because various points on the ‘secondary sruolure are allaciad to one another. The stongest Sinks are caused by bonding between naighooing eysteine ano ‘acids which form aisulide bridges. Other interactions that aro ‘evolved in folding incude weak ionic and hycrogen bonds as wl as hydropobic interactions Quaternary Structure - 4° ‘Some proteins (such as enzymes) are complete and functional wit @ terry stucture ony, However, many complex proteins ‘exis as aggregations of polypeptide chains. The arrangement of the polyaentide chain ino & functional protein is termed the quatornary structure, The examole (ight) shows a ratecule of hemoglobin, lobular protein composed of 4 polypeptide subunits roned together: two identical beta chains ard two konica! alpha ‘chains. Each has a heme (ron containing) group at he centr ot the chain, which binds exygon. Protons containing non-protein ‘material are conjugated proteins. Tne non-prtoin partis the prosthetic group, Denaturation of Proteins Denaturstn refers tothe loss ofthe ttee-disensional stucture (71 usually also the biclogcal functen) of a poten. Denaturtion |S often, athough not alvays, parmanent. It esulls from an aeration of the bonds that maintain the secondary and toriary sucture ofthe protein eventhough the sequence of amino acids remains unchanged. Agents that cause donaturation are: "Strong acids and alkalis: Disrupt Ionic bonds and result in coagulation ofthe protein. Long exposure also breaks down the primary elwature of he proten, ‘+ Heavy metals Nay isnt onic bonds, form strong bonds wth te carboxy! groups ofthe groups, are ede poten charge ‘The goneral elect i to cause th preciptaon of he proven + Heat and radiation (o.9. UV): Causo dsruption ofthe Bonds Inthe protein trough hnovesced energy provided to tho atoms. + Dotergonts and solvents: Form bonds with the non-polar (groups Inthe protein, thereby disrupting hydrogen bonding RA2 precise structure (denaturation), it is usually unable to carry out his Biological tuncton, Proteins are often classfied on the basis, ‘of struotura (globular vs fibrous). Some of the properties used for the basis of structural classification are outlined opposite. a [> amnoscts ‘Amino acid ‘sequence 2 Hydrogen onde i ‘To allel shape Iemastained wit hysiogen bond we peptise crane Alpha (a) helix or pleated shoot iste ree Beta chin 148 cing aside [pha chive 181 amine sede Inberresioin, each Polpeatle encloses anon ‘oniaining poset group Hemoglobin molecule Homogtobin's Chemical Formula: | Cae H ser O era N aap oF, Photocopying ProhibitedFibrous Proteins Properties + Water insoluble Function + Structure + Contacte 29. myasi, ect CCotagen consists ofthe polypeptides wound around each ‘thor to form a rope’. Every third ‘amino acid in each polypeptide is @ ‘lycine (Gly) molecule. wher frykegen berdng ocous hldng the ties sande together. + Very tough physical; may be supple or strotchy + Paral polypetie chains n fon fiers or sheets cells and organisms «9. colagen ‘und in connective lssve, catlage, bones. fendons, an bivod vessel wats heteal bers frm due 10 ‘ose linus bataen ‘lagen motels. Globular Proteins Properties + Easily waler soluble + Tortary svete eral to furetion + Polypeptide chains folded into a spherical shape Function + Cetalyic 2g. eneymes + equator eg hormones (insuin) + Transport eg. homogiobin| + Prolecive eg, antbodies cee eee wey Bovine insulin i a rolativety mal preteln consisting of two aolypeplde chains (an chan and a car), These ‘wo chains ave held logetner by dislide bridges between neighboring cysteine (Cys) molecules. 1. Giving examples, briefly explain how proteins are involved in the following functional roles: (@) Structural tissues of the body: (0) Regulating body processes: (0) Contractile elements: (2) Immunological response to pathogens: (9) Transporting molecules within cells and in the bloodstream: () Catalyzing metabolic reactions in cel 2 Explain how denaturation destroys protein function: 3, Deseribe one structural difference between globular and fibrous proteins: _ 4, Determine the total number of amino acids in the « and chains of the insulin molooul ilustrated above: (@) «chain: Photocopying Prohibited (©) B chain: é a Fs 3 fal g i 3 a 9 Me PSE eB BT x Ye Mae ty % Mu » ils 4“ hie b = & Vin Bae"8 ey BY PE ES a ag 1. (@) Explain what a glycoprot Modification of Proteins Proteins may be modifad after they have been produced by ribosomes. After they pass ino the interior of rough endoplasmic. reticulum, some proteins may have carborydrates added to them to form glycoproteins. Protoins may be further altered in, the Golgi apparatus. The Golgi apparatus functions principally as a system for processing, sorting, and modifying proteins. Proteins that are to be secreted from the cell are synthesized by Nea alprtenssyntesized by flsoeomes bound lothe endoplasmic reticulum acauire exbeyate uns {hataretached ta them, Proteine made by ree EP Carbatycrat groupe may al 36 marker hat ‘elerrine th Gaslnalin a gloopatan win ho ‘calor for export The extotystalee may bo moved ‘her the proton nas reached is etal. Ccartctyetae groups may help positioner orientate aveopotins In membranes. The earbohyarate gous prevent fem fer rotating te membrane | Glycoprotein byte immune syston, conan % 7 N27 ‘ycopretein| () Brietly describe three roles of glycoproteins: ‘Nbosomes Inthe cjtca ere ios deed of eaboryseate a ° 1 ctr nye mb iteracoon of eteron cet form {esues and the cotton of orsign els ‘ wl by ribosomes on the rough endoplasmic reticulum and transported to the Golgi apparatus. At this stage, carbohydrates may be removed of added in a step-wise process. Some of the possible functions of glycoproteins are ilustrated below, Other proteins ‘may have fatty acids added to them to form lipoproteins. These. ‘modified proteins transport lipids in the plasma between various, organs in the body (e.9. gut, ver, and adipose tissue). Branching chains of carbeytes are ede ‘pot ferent nas of gars linked together omer Cita sector ofa cat ecognlion Eningod eookon of plasma membrane ‘showing a lyoorte embeded ini 2. (@) Explain what a lipoprotein is: (©) Brielly describe the role of lipoprotein Suggest why proteins made by free ribosomes in the cytosol are usually free of carbohydrate: Suggest why the orientation of a protein in the plasma membrane might be important: 7 Photocopying Protbited tyBiochemical Tests Biochemical tests are used to detect the presence of nutrients, such a lipids, proteins, and carbohydrates (sugar and starch) in various foods. These simple tests are useful for detecting hutrents when large quantities are present. A more accurate technique by which to separate a mixture of compounds involves Praca ane Set Up and Procedure “The chromatography papers folded so it can be secured by the bung inside the test tube. “The bung aio prevents the solvent sporting. Chromatography paper may be treated with chemicals to stan normally iwisible pgments, ‘A pot of concentrated samples added using ' pipet and suspended above the solvent ‘As the solvent travels up the paper Iwi carry tha sample with i Tha distance the sample ‘ravels depends on its solubility. ‘A panelling used to show the starting point Solvent Determining Rf Values “To ident tho substances in a mixture an Ry value le caleulated using the equation Distance traveled by the spot «) ’ Distance traveled by the colvent (y) x ‘Those Ry valuss can thon be compared with Ry values from known samplas or standards, 1 | forexamplo: Gilycne’s Fy value = 0.60 Alanine's Bj value = 0.70, ‘Aaginine's Ry value= 0.72 Leucine's Fi value= 0.91 chromatography. Chromatography is used when only a small ssemple (s avaliable or when you wish to distinguish between nutrients. Simple biochemical food teste will how whothor sugar |s present, whereas chromatography wil distinguish between the sitferent types of sugars (2.9. fructose or glucose), Reagent: Blurot solution, Procedure: A sample is added to biuret solaton and genty hested. Poste result: Solution tuns from blue to lie, ‘Starch: The lodine Test Reagent, lodine, Procedure: _lodine solution is added tothe sample. Positive result Blue-blackstaning occurs | Lipids: The Emulsion Test Ethanol, ‘The sample is shaken with ethanol. After setting, he quid portions dstiled anc med vt water. Positve result: The soluion tus nto couxy-ehite emulsion ‘of suspended lipid molecuies. Reagent Procedure: ‘Sugars: The Benedict's Test Benedlts solution. ‘Non reducing sugars: The sample Is boled ‘wih dist hydroctlorie acid, then cooled and neuitaized, A test fr reducing sugars is then performed, Reducing sugar Benadics solution's added, and the sample is paced in a water bath. Positive result: Solution tums from blue to orange. Reagent: Procedure: 41. Calculate the Rr value for the example given above {show your working) 2 Explain why the i value of a substance is always less than 1: 3 Discuss when itis appropriate to use chromatography instead of a simple food test: 4, Predict what would happen if @ sample was Immersed in the chromatography solvent, instead of suspended above it: 5. With reference to their Fr values, rank the four amino acids (isted above) in terms of their solubility 6, Outline why lipids must be mixed in ethanol before they form an emulsion in water: BS rac fal els x mee ss og ae Vebe 2 Ms Ly)rs FPR? t 3 RY PES. BAI Ve EEC SIGE “ Oy, a ee EVES aE Cod Enzymes Most enzymes are proteins. They are capable of catalyzing {speeding up) biochemical reactions and are therefore called biological catalysts. Enzymes act on one or more compounds, (called the substrate). They may break a single substrate ‘molecule down inio simpler substances, or join two or more, substrate molecules chemically together. The enzyme tse |s unchanged in the reaction; Ils presence merely allows the reaction to take place more rapidly. When the substrate attains the required activation energy to enable it to change into the product, there ie @ 60% chance that it will proceed forward 0 form the produet, otherwise it reverts back to a stable form of Enzyme Structure ‘The model on the right is of an enzyme called Ribonuclease 5, which breaks up RNA molecules. Is 8 typieal enzyme, being @ globular protein and composed of up to severe hundred atoms. The darkly shaded areas are called active sites and meke up the cleft: he egon nto which the substrate molecule) are raw. The correct posting of these sites is tical forthe eatayc reaction to occur. The subsrato (RNAin this ease) is drawn into the elt bythe active sites. By soing so, It puts the substrate molecule under sess, ‘causing the reaction to ptaceed more readiy. How Enzymes Work ‘The lock and key model proposed earlier this century suggested that the [ subsrate was simply drawn into closaly matching ciefon the enzyme molecule, i More recont studies have revealed that the process more likely involves an Induced ft (sco diagram cn the right), where te enzyme or he reactanis change ‘thoi shape slightly, The reactants become Bound to enzymes by weak chemical bonds, Ths binging can weaken donde vithin the reactants themeoves, allowing the reaction to proceed mors ready. Enzyme ‘The presence of an enzyme simply makes it easier for a reaction to take place, All eatalysts spood up reactions by influencing tho stabilty of bonds in the reactants. They may also provide an alternative reaction pathway, thus lowering the activation energy needed for @ reaction lo teke place (see the graph below), Ai & € €> the reactant again. The part of the enzyme's surface Into which the substrate 's bound and undergoos reaction is known as the ‘active site, This is made of diferent parts of polypoptide chain, folded in a spect shape so they are closer together. For some ‘enzymes, the complexity of the binding sites can be very precise, allowing only a cingle kind of substrate to bind to it. Some other ‘enzymes have lower specificity and will accept a wide range of ‘substrates of the same general type (e.. lipases break up any fatty acid chain length of lipid). This is because the enzyme 1s, ‘specific forthe type of chemical bond involved and not an exact substrate, Substrate molecule: Sutsate roles are the cml that ‘enzyme acs on Tey are crwm info tne et fhe enzyme, Active sites: These tacon point dat ‘me abate to he enzyme euace Substrate molecular pestioned na ‘sao prove reason ele ning tao melsedes ogee a splttrg una larger one (esinihis case). Enzyme molecule: The company of the acne she wr makes each rayne so specie precsoin terme a the Szosvate 18 0) Induced Fit Model ‘An enzyme fis nits substrate somewhat | ie’ lock and ey. The shepe ofthe fezyine changes wien the subst fs Into te det (ated ne induced ‘the lato the enayne ‘witnout enzyme: The onary requres forth actor fo procs {onward drctn (he acvaton onary) [shigh wthout he enayma present : nine “The nye changes shape ong the edstate molecule to comono : an ane wh ) : enzyme: The ctvaon ener al Isreducedby tho presence of he ee be rayon reer turn st : S 58 rotors more ess ex EF Presse g © Beputrocnspato mene enzyme fic eure i eneray eral sage eae oreo mer oa ‘Drecton af scion feat ee eno rata! 2812808 a Paotocopying ProhibitedStxite thease eae Taare Baan end ee morte See seo Surtneaet Stance Mics | nace me ta [ breaking of bonds. Ai rp eee Catabolic reactions ‘Some onzymes ean cause 2 single substrate metoculs to be ‘awn into the acive ste, Chemical Bones are broken, causing the substrate molecule to break apart to become two soparate molecules. Examples: digestion, celuar respiration The we susie moeciles tre atractd ice enzyne bythe active sites “Trotwn substate molecules form a single prouct and ae roland alow the onayne oars OC RS} satin entomte Sunjctod io aess ee ‘hich it ai the 7 ‘ormavenotbonde Anabolic reactions ‘Some enzymes can cause two substiata molecules tobe drawn Imo the acive sit. Chemica bonds ae formed, causing te tO substrate molecules to form bonds and become a single molecule Examples: protein sythasis, photosynth, 1. Give a brief account of enzymes as biological catalysts, including reference to the role of the active site: 2. Distinguish between catabolism and anabolism, giving an example of each and identifying each reaction as endergonic or exergonic: 3 Outline the key features of the ‘lock and key’ model of enzyme action: 4, Outline the ‘induced fit! model of enzyme action, explaining how it differs from the lock and key model 5. dently two factors that could cause enzyme denaturation, explaining how they exert thelr effects (see the next activity} (@ o 6. Explain what might happen to the functioning of an enzyme if the gene that codes for it was altered by a mutation: ene mathe! 20012005 Photocopying Prohibited WG vit a SP Oue ote eke S}et al eae wy PRAT ee ee VIG we Enzyme Reaction Rates Enzymes are sensitive molecules. They often have @ natrow range of consitions under which they operate properly. For most ‘of the enzymas associated with plant and animal metabolism, there is litle ectivty at low tomperatutes. As the temperature Inereases, s0 too does the enzyme activity, until the point is reached where the temporatura is high enough to damage the enzyme's structure, At this point, the enzyme ceases to funetian;a phenomenon called enzyme or protein denaturation. Extremes in acidity (pH) can also cause the protein structure ‘of enzymes to denature. Poisons often work by denaturing tenzymes or occupying the enzyme's active site so that it does, rot function. In some cases, enzymes wll not function without cofactors, such as vitamins or trace elements. In the four graphs below, the rate of reaction or degree of enzyme activity is plotted ‘against each of four factors that affect enzyme performance. ‘Answer the questions relating to each gtaph: 1, Enzyme concentration (@) Dasoribe the change in the rate of reaction when the enzyme concentration ate of eacton ‘wh fxd amount of enzyme ‘and apie cofactors present — ‘Concentration of subse 8. Temperature A e BT] wont me ea see samy Fee seo 4. pH (acetyl A oot : (b) Explain why the rate changes the way it does: _ (0) Pepsin acts on protein to Its working environment: A is increased (assuming that substrate and cofactors are not limiting): 5 sass 2 a With ample substrate (©) Suggest how a cell may vary the amount of enzyme present in a cell: and cofactors present ——__—> Enzyme concenzaton oo 2. Substrate concentration (@) Desoribe the change in the rate of reaction when the substrate concentration A is incteased (assuming a fixed amount of enzyme and ample cofactors); Higher temperatures speed up all reactions, but fow enzymes can tolerate temperatures higher than 50-60°C. The rate et which enzymes are denatured (change their shape and become inactive) increases with higher temperatures. (e) Describe what is meant by an optimum temperature for enzyme activity: (©) Explain why most enzymes perform poorly at low temperatures: ity) Like all proteins, enzymes are denatured by exiremes of pH (very acid or alkaline). Within thase extremes, most enzymes are sill influenced by pH. Each enzyme has a preterred pH range for optimum actly {a) State the optimum pH for each of the enzymes: Typsin: Urease: _ the stomach. Explain how its optimum pH is suited fo Cad ‘Photocopying ProhibitedEnzyme Cofactors and Inhibitors Enzyme activity Ie often influenced by the presence of other and may be organic molecules (coenzymes) o: inorganic ions chemicals. Some of these may enhance an enzyme's activity, (e.g. Cat*, Zn). Enzymes may also be deaciveted, temporarily Called cofactors, they area nonprotein component ofan enzyme or permanently, by chemicals called enzyme inhibitors, ‘Types of Enzyme Neary al eraynes ae ade of 3 prot ssough RNA boa been aoe as sete to ? Scmertttated fe have cnayae — Bee properties Some enayree cont mS) comes — \ 2 Erie poten, whe cher eaiee Soren Fy tho addon fra congonen cay ee 8 comes tar cate poperien Fa These aye permanent acd soon E paris called prosthetic groups, or ‘Apoenzyme = oral allaches Paces Enayeconpiee_Prothale gfoup roqured Coenzyme required By {Goenaymes) that van ater & ey pot, Contaneapcouame pris) Caine spoon (ae) = {tector ad may oars th cee nae spomrae Sanne geen te) 5 aneiner enzyme noe actors. to teepaie AD 9 shyeegetaee © NAD Roversible Enzyme Inhibitors Ireversibi inhibitors (Poisons) | gy! compan Trenunte = “a 2 The straint euseas —~ @i cutdnin artis Reaseromrsic, (BN Tne ' fmesters) CB ecae mabe & Geass CR) tale 30 = BU ewer, | Mveeyate Noo ri or tion | SER g ee wehtoeee / home * knyne enme Paar om at sepa ‘eremoetine 4 sor ns Cota ney malting oy and permanemiy to the active sos of “a Hoiniaion Compete Noncompative Alot nayno met nome secs en Peapeetavoyn re cutie i provers Beagle ote hea a Petia ete cam (C8), 0d nay titre my be ees or inevesBe. Reverie ios ae med oct | (Poh meron Oh ent aon Ml rcynsctity. Ture buen on recon etneo ie ssa end pod endth names | Thy ae gunealynon-ampetive } ‘controling the reaction. Bulldup of the end product ora lack of substrate may serve to deactivate inhibitore, athough moroury is. an a the orayne Ts ceacvaton ney ase he forme competve (computes forthe active ste) or | exception ané deactivates. the - orcorpetiive rhaiton Ue nonconpetve iioiers av th eso ng Gown the te | onzyna papain. Hesny metals are “ {Frmccln allosteric iors Bock ace se atogeter nd pve ts ursodg feted boty a oe sony ” ag |. Describe the general role of cofactors in enzyme activity: aes 2. (a) List our heavy metas tha re tx to humans x (b) Explain in general terms why these heavy metals are toxic to life: a e 3, There are many enzyme inhibitors that are not heavy metas (9. hose found in some pesicies}. ; {@) Name @ common potson that isan enzyme inhibitor ut rota heey metal 4 (©) Try to find out how this poison interferes with enzyme function. Briefly describe its effect on a named enzyme: at “ x “4 4. Distinguish between competitive and noncompetitive inhibition: a wf 5. Exiain how allosteric inhibitors dif trom ether noncompeie inhistors : * * Photocopying Prohibited fol Co) wd bveraties 2001008SF & Ww ed *e ES Wen Humans have used enzymes for thousands of years in food land beverage production, but the use of enzymes in industry | a comparatively recent development. Many industries now rely on the large soale production of microbial enzymes to catalyze a range of reactions. In the absonce of enzymes, thes reactions sometimes require high temperatures or pressures 10 proceed. Industrial enzyrmes must be relatively robust against denaturation and capable of maintaining activiy over a wide temperature and pH range. Enzyme technology involves tho: production, isolation, purification, and application of useful enzymes. Commercial enzymes are produced from three main © coon of te microorganisms: ‘cle fareroraytom an entoced stare system ‘tain cure broh i hich he moore {bacterin ertingy se gown url ho oxtacarpreits {crthe cote hae) nav accureled fo: haves. ‘Sondtonsinine temanter vessel re cosely montored Sno careay equate so tae condos for mata mero grow ae ortiz Te model ih shows 2 catanaysecton of cial ‘ermenaton chamber cao ht vd or contri tobi outros © seperation Drum stration separates ‘he Sompunens fhe ferme vat — Producing Extracellular Enzymes, CCuture meu anc secreted fexraceils) ‘onermes ‘Concentration: The ‘eeyia coluionis| onontates by ‘reducing ts wator coment 09 by reverse comes. Preservation: Antbactrl ‘agonis ee added atti siege to prevent contaminate. y Purteatin and processing “The crue enayme product. may be ded prods & pons or futher puted by ‘recipatoneretaleaon or ‘atorpon (gent cys) Industrial Production of Enzymes ‘sources: plants, animals, and microorganisms (mainly bacteria, ‘and fung)-Most enzymes used in industrial processes today aro ‘microbial in origin and are produced in industrial-scale microbial {fermentations using liquid or semi-solid grown media. Note that, the term fermentation, when used in reference to industrial microbiology, applies 10 both aefobic and anaerobic microbial growth in bioreactors. Generalized plans for the industrial ‘production of oth extracellular and intracellular enzymes. are lystratod bolow. Note that the isolation of intracellular enzymes. (below, right) is more complex because the cells must ist be Cisrupted to release the enzymes within. Fat bladed turbines ‘asta nuent ‘mediomand meres Prebes monitor Shangos in he — ‘postr enone ‘Teomal acket $-——mamains goth [terest ‘base dieporses tele a eough ecalve medium cee resting tn Producing Intracellular Enzymes Diszupton: Once ho cos rave Bsan = ‘separated tom te ulire madi, ey ‘rust be supted (sing ulrascund) © release the enzymes win he cl @ Coniitugstion: tho cota debris remaning ate dsapton removed by centtugaten (rian). Y Puritieaton and processing: Insalputeaton Ivo postion tn ammonium sua 07 erganic Sovents Fura: putceton aco by Ton exchange chromatography or 90 loorophorecte. 41. The industrial production of microbial enzymes varies according to the enzyme involved and its desired end use. Compare the two flow diagrams, for intracellular and extracellular enzymas, above: (a) Explain the main way in which the two production methods differ: (0) Suggest the reason for this difference: 2. Enzyme solutions can be packaged and used as crude extracts without further purification (8a). State one benefit of this: fet. ‘Photocopying ProhibitedPutting Enzymes to Use Depending on the way in which the desired end-product is free enzyme extracts are more axpensive ta produce, but ean produced, enzymes may be used as crudewhnole cell preparations be a more efficient option overall. Ta reduce casts and improve fr as cellree enzyme extracts. Whole call preparations are the eiclency of product production, enzymes are sometimes: cost elfective, and appropriate when the processes involved immobilized within a matrx of some kind and the reactants are. in production of the end product are complex, as in waste passed over them. The various methods by which enzymes are treatment and the production of semi-syntnetic antibiotics. Cell put to work are compared in the diagram below. » ; Fa Advantages Disadvantages Methods of Enzyme immobitzation ra renopaation 9 Coltrae Thana ght __‘Te sane nye vated as 3 Staymo enact Jenjoo soni eh tony tur oce Tesoro tevin IR Enayrne is used in enzymes are free in schution, “The end-product is not enzyme alginate or ie Sue feeont ney eee pamcramecapede, Lattioe entrapment 3 Enno repped a geltmen gta. = | tmmobitzsd Theerayrascanbosed Ty onepnnt cess may pres tnzyine, rpeenyansmenmacessly asolne ono say (raton saci Enayne steldin CS vodues costs) (ror eraymo 6 bo naeded), nae SHURA ee anaymtnetpatit Sone menos ten neh Ens ne « is casdy harvested. -stabiliy (@.g, covalent bonding) pa “The enzymes are more stale are haere achieve - Gieloropeedionc enti mnebmaton nb sspansUSELALETeee Enzyme ‘Covalent attachment eet “reo o sane names. Enymetoconlenty ‘a Fokmen steno an tondete saa £ immobilization. substrate, surlac 0.9. colagen é egecliagen YO ra synthtc polymer. & Uscdtrernmesthte Lessin andmowrand te as Whole coll tnetabe erinecivatad when han frst producing 3 pUD Direct crosstinking | Preparation wee en tt pon Gatrsydeedto wo fiat cas ny ‘root cree Tein” Uae ccamplr rotstes —Somed th ebsanin ned See apace ; (Sting nore han eve ‘eemusenl grony ste Tecra “a ‘nveolor econ Pcoar les oto oer Sine srr oe 1. (@) Explain one benefit of using a cell ree enzyme extract to produce a high-value end-product: {b) Identity one factor that might be important when deciding not to use a coll free extract 2. (a) Deseribe two benefits of using immobilized enzymes (rather than enzymes in solution) for industriel processes: (0) Describe a cisadvantage associated with the use of immobilized enzymes: _ {c) Describe a factor that would affect the rate of end-product harvest from immoblized enzymes: 22 an ‘8. The useful Ife of protease enzymes is extended when they are immobilized (as opposed to being in solution). Using a what you know of enzyme struciure, explain why immobiization has this effect in fis case: "| 4. a ims E i asl 4. Suggest why immobilization would reduce the activity of certain enzymes: 4 4 - - * Cras oc raw3 ye ZN s 8 aN ED, TSF e Ss Microbes are ideal organisms for the industial production of zymes because of their high productivity, ease of culture in industrial fermenters, and the ease with which they can be genetically modified to produce particular products. In addition, Oy, in beer browing, proteases (rom bacleria) are ddd to provent Govsinees. Arpoglucoldases are odin prose bw cae bees. Enzymes sv used in varus stapes tenes production, e9. cwmnosn ffom GE mrobes nom replaces the ‘orm prove tana rom cas. fd paper Industres oreo lromwood pupand tea ood waste epilnaae from Stplonyeos sp. duos trom old photographs can be reciaimas Fouse wnen proteases ae employed tocdgest te goat of od Fins CCaluloses ang pectnasee are used Inte menuacore of packaged fas ‘ppoted Wes) uees'9 speed Ie execcton ad peer coves. ‘Tre enzyme, ghieose oxidase, for Aspe rige,isimmobiizad ina ‘emicerdictin sleanch tease {he comrsen of luce (rom ne Diced arp) ganic. Paste sleeve penraabole glues Bouse say wed fon Some of the many applications of microbial enzymes in medicine, industry, and food manufacture. ydrogan on rom he ghcone acl cause ‘mavemant of acon tha seer, wich Is cotecte by atvaneducar. Te evenain of tha lacie cures recy proportonal 0 the blood ghitose cancanratin. | resp imped ‘Transducer mr Ampliier Applications of Enzymes becouse there is an enormous diversity in microbial metabotism, the variety of enzymes available for exploitation Is very large. ‘Some of the microorganisms involved in industrial fermentations, ‘and their enzymes and their applications are described below. tga! torent uo proteases, ‘pane, er omjsses exacts Work ung: and thermore bacteria to break oun onanismatenal mals, Ciesla used in jam prosction odie ynthesbadty amutet sae ha igi Aspois niger fh ‘rosie teensy lets ease Insoft centred hocolates. verso tremyoast bea down he soto 19 ro proguco he softcore. facial prtoasos ae vod to break ‘wn the eat prot (lun) in Aur te produce fw gto breads. <@ ‘Tre ince tom bacteria is used to convert lactog> to qlucote. ard (alacioee in the preuon off Fates ane nts fe ak prods wing nustios now use potenses from Baclive eu stea of oxic chomosla ech auld pastes, 10 ‘move hats ane ston Pi. eau sre sown ‘tigi oye dapiay Blogensors are laconic montring doviees| ‘hat use bose materiale dotnet he prosence fF concentiation of @ particular substance Enaymes are cea sud or use nbiosensors ‘because o her spect and sensitivity This ‘example ilueratos how glucose oxidase from the ung Aeporpivenigors used na bisoneor ta messuce blood glucese level in diabetics. ‘ecirane etamatana 20012808 Photocopying Prohibited|. Identify two probable consequences of the absence of enzymes from a chemical reaction that normally uses them: @ (b) = Identity three properties of microbial enzymes that make them highly suitable as industrial catalysts. For each, explain ‘why the property is important: “ @ Fy 2 - - a 3 © 3 - Pa © g cy ‘Choose one example from those described in the diagram opposite and, in more detail, identify: (@) The enzyme and its specific microbial source: we et * (©) The application of the enzyme in Industry and the specific reaction it catalyzes: M =. * ACS xt 1. (@) Outline the basic principle of enzyme-based biosensors; ’ (b) Suggest how a biosensor could be used to monitor blood alcohol eve: : Vere 3 x ae Weak . For each of the examples described below, suggest how the use of microbial enzymes has improved the efficiency, cost effectiveness, andlor safety of processing compared with traditional methods: ty ‘ (a) Use of microbial proteases to treat hides in the tanning industry: hh 2 tN (b) Use of microbial chymosin in cheese production: ® {0) Use of fungal igninases to treat wood waste: icone matin 001-2005 4 Photocopying Prohibited s