A brewer’s biochemistry This is the first of a series of articles aiming to position malting and brewing in bio- chemical terms for the benefit of those who have received no training in this area of science. In fact no formal scientific training is assumed in the reader so some basi chemical principles are included in an accompanying FactFi Part 1: Proteins Proteins play a number of ertical roles in nature. These include: ‘structural roles (e.g. the collagen found in ‘many issues, including the swim bladders of fish tat end up asisinglassfnings) the carrying of ether molecules around (09, the transport proteins which have a role in selectively moving substances across, membranes, such as the membrane around ‘eewing yeast) ‘imparting mobity (e.g. inthe whip-the fag la found on certain spaling micro-organisms and which propel the beasts along) ‘© orotection, as antibodies that are produced by higher organisms In response to the Presence of “foreign* materials (such anti bodies ae increasingly widely used in selective {ests for certain materials of interest to the brewer) ‘catalyse. Here | am referring tothe enzymes, incluaing those from mat and yeast, which are ciitical in the brewing ané fermentation Processes Amino acids Proteins are polymers (see panel in FactFle) of amino “acids. Amino acids. are. so-called becnuse thay have an amino group (NH) and mexyl acid, (-COOH) group. There are twonty of them commonly found in proteins and ‘Wey share a general formula: ir H¢-000H R Each amino acid has a different ‘group, ‘These are shown in Figure 1. The simplest, in siycine, comprises a solitary H atom. Others, such as that in tryptophan, are quite complex. The properties of these R groups impact ‘greatly on the proparis of the individual amino acids, bt also on the properties of proteins in which they are found. The oddity is proline, wich inthe strictest terms is not an amino acid (60 | show its full formula), butt obviously has close similares othe amino acids Both the amine group and the carboxy group cof amino acids can become charged (see FacfFle). Carboxy| is an acidic group, i. i releases hydrogen ions (H*).Aming is a“basic™ ‘group because it accepts hydrogen ions: If the pH is very low (high concentration of 1), then the carboxy! group wil tend to bein the uncharged form (COOH), whereas the ammina group wil tend tobe inthe postive ionic form (-NHs"). The converse applies at high pH. For intermediate pH's the majority of tho molecules will have both a positve and a negative charge ~ they are apolar. wf-coon Eco ecco This abilty of amino acids to alternately “soak up" and release H* means that (within, limits) they are able to regulate the pH of solutions that contain them ~ ie, they are buffers. As such they play an important role in regulating the pH of wort and beer. Peptide bonds I two amino acids come together, then a ‘molecule of water can be spit out betwoen them and a bond formed that joins. thom together. Tisis called a "peptide" bond (boldin th diagram): a Fa | 4HN-C-COO. *H4N-C-COO- | | 4 H he ° R HNC 4 zo Rr -N-C-COO" HH The product is @ dipeptide. This reaction is reversible: by adding water, the dipeptide will be spltnt its corresponding amino acids “There area very large number of posses for dipeptides. For any two amino acids, there are two dipeptides. Take glycine and alanine for Instance. The first dipeptide will have the peptide bond formed Between the ~COO” of alycine and the -NHs* group of alanine. The ‘secand has the peptide bond formed beiween the ~COO’ of alanine and the -NHs' of glycine. Thay are quite distinct, have thelr own properties. Convention has it that peptide structures are weil withthe free (unbound) ‘amino group to the left and the tree carboxy! {group (the one not tied up in a peptide bond) to fhe right. Thus tha frst of our dipeptides would 'be glyey-alanine, The second would be alany! sicine. ‘There is essentially limitoss scope for more ‘and more amino acids to be joined on to the Chal. Broadly speaking if there are between 2 ‘and around 10 amino ack in the chain then we have @ peptide or oligopeptide. It there are more then we have a polypeptide, In those polymers only one of the amino ‘acids has a free amino group (apart from the amino groups in the side-chains of certain amino acids, see Figure 1) and this Is called the ‘Neerminus. Similary only one amino acid has free carboxyl group (apart from the carboxy! ‘9r0ups in the side-chains of glutamate and aspartate, see Figure 1) and this is called the Corminus. Most polypeptides found in nature contain botween 50 and 2000 amino acids. The average molecular weight of an amino acid is approx. 110, so the molecular weight of Polypeptides may be as much as 220,000 (220K). (It seems to have become the norm to insert the word “daltons” after. molecular weights, in honour of the Manchostor-based professor who did the pioneering work on atomic structure, This is strictly incorrect, as ‘molecular masses are unitess. They are ratios cof size on a scale that sos the smallest alom, ace age oft Fig 1 The side-chains inamino acids rug + Mareh 2001,cued Gy Or op OO, of 900, © Hine! 6 by ‘Om, Fig 2 Tonic bon, Fig 3 Hydrogen bonds, hydrogen, with a molecular mass of one.) The sequence of amino acids ina polypeptide chain is called its primary structure. Wis tis iwhien determines the properties of the polypeptide, for the simple reason that the folaing ofthe polypeptide chain is determined by the opportunity for amino acids in diferent regions ofthe chain to interact. This folding is referred to as secondary and tertiary stucture. ‘Various forces dictate these interactions. There may be strong altractns between positively and negatively charged groups inthe side chains of the amino acids ~ as every schoolchild knows, opposites attract, 1. positive attracts negative, Equally, ike charges repel, so that postive repels positive and nogative repels negative. ‘And thus the Impact of his on the shape of a proteia molecule depends on how many ofthe ‘amino acids are present that have these ‘charges on their side-chains. It also depends ‘on what the pH ls, as this wil influence the proportion ofthe groups that are present in a charged form or an uncharged form (soo earl Ifthe condions ae right, then it may be that ‘amino acids quite a long way apart in the molecule come close together and are “cemenlad” by these strong ionic interactions (Fig 2). In this way the polypeptide chain ‘adopts a certain shape. (Other interactions can oceur, Some of the most important are called hydrogen bonds, ‘Sufi to say (and for reasons that wo nacdn't {99 info) in the chemical grouping containing ‘one oxygen and one hydrogen (i.e, -OH, the so-called hydroxy! group) the oxygen atom is slightly negatively charged and the hydrogen atom is slightly positively charged. Therefore if two soparate -OH groups come close together there can be an interaction between their respective positive and negative regions (Fig 3h ‘Individually, these hydrogen bonds are ‘weaker than the fuly-ledged postive-negative ‘bonds refered to above, but cumulatvely they ‘ean be very significant. Similar bonds can ‘occur with N-H groups. Infact hydrogen bonds. involving -OH and -NH groups are responsible for tha coillng of same regions of proteins rather in the way that the cord linking a © sophaicanto Fig 4 The pes of interactions responsible for 3-dimensional structure of polypeptide chains telephone receiver tothe main unit twists nto a helix, Altematively these bonds can. link adjacent regions of proteins into sheet forms. This hydrogen bonding is most marked in water, where ofcourse thore are los and lots of “OH bonds and whole network stuctures can be formad between adjacent molecules. W's a very cosy situation - and apart ver icut to break up by inteuder molecules and groups. Examples ofthe latter types of group are the ‘amino acids with hycrocarbon side-chains (Le. those amino acids who's side-chains are ‘emtialy composed of C and H) “They cant make hydrogen bonds and so they are “excluded trom the club”. n fact thoy tend to be banished to the inside of protein ‘moloouios where they associate together. They are referred to as hydrophobic amino acids, because of this “water-hating” tendency. tis the hydrophilic groups that predominate onthe ‘outer surface of he proteins because thoy can pal on" withthe water molecules —for example the -OH group of serine is perfectly able to hydrogen bond with water. ‘Another lype of bond that determines the shape of protein molecules is the so-called ‘sulphide bridge. Amino acids containing ~SH side chains may come togethor with the hydrogen atom of each being removed as the two sulphur atoms link. The bond formed Is ‘even more resistant to breakage than an ionic bond and in some proteins thase bridges are very important for determining the overall shape, Fig 4 gives a hypothetical picture of how these various types of interactions determine the shape ofa protein molaculo. You need totry to imagine these things happening in 3: dimensions - we are dealing with essentially spherical stuctures — Le. fotballs rather than Frisbees, ‘So why does protein structure matter to the brewer? lteaters for various reasons, Enzymes Let's start by considering the enzymes that are {0 important for producing brewer's wort and hich are presentin the yeast where they actin sequence to convert sugars into alcohol Enzymes ae all proteins, each of them capable of effacing its own specie reaction. Amvlases Mareh.2001 + The BREWER froin + wwighorp ak ' —7 £ nem conenatin ‘exclusively break down starch, 8- FFig5 The qlucanases break down f-qlucans, Flarionship. proteinases break down proteins, Between and soon Enzymes ara __ biological catalysts: molecules present in all ving ‘organisms that are responsibie for speeding up the reactions occurring in those systems (see FactFile). The molecules that they act on are called substrates, the molecules formed are products. The more enzyme available, tho fastor the reaction, We can liken them to turnstiles at a football ground: the more there are, the quicker can customers get through. The relationship between the speed of an enzyme-catalysed reaction and substrate concentration is not so simple and the relevant graph usually has a shape like that shown in Fig 5. At a certain ‘substrate concentration the system becomes. “saturated”: inereasing the substrate concen: tration no longer causes the resction to go any faster Tho explanation i that the enzyme binds on to the substrate motecule to form an “enzyme- substrate complex’. This thon breaks down to re-orm the enzyme (ready to grab another substrate) and release the product. This binding occurs atthe so-called "active site’ Thore is a unique shape in each enzyme molecule that recognises the substrate, The shape ofthe protein molecules determines this. niche, by tie way In which it folds on lself through the Interactions I described ear. Its rather like a space module docking with the ‘mother ship. AUS module needs a US docking port, nota Russian one (by and iarge!) The active ste might comprise amino acids from quite distinct pars ofthe enzyme molecule (Fig 6), As onzymes are relatively flimsy, anything which wil tend to drva these amino ‘acids apart wll disrupt the active site, prevent ‘substrate binding and destroy enzyme acivily. ‘Sueh factors include heat which causes the protein to jiggle about uni it loosens up, and changes in pH, which alter the proportions of positive and negative groups in the proteins ‘and therefore the opportunity forthe charge ‘charge Intactions which hold the shape of he ‘molacula. These are the reasons why extremos fof temperature and pH are to bo avoided, Enzymes differ in their tolerance of temperature and pH 'As well as thir affect on the integity and “survival” ofthe protein molecule, temperature and pH also impact directly on the rate ofthe reaction that the enzyme catalyses. All chemical reactions are accelerated by heat, withthe rle of thumb being that a 10°C rise in temperature speeds up a reaction by 23 ol This applies to reactions catalysed by enzymes, with the important rider thatFig6 The concept of “active ste” increasing heat will also tend to disrupt the fenzyme structure, deform the active sita and therefore prevent the enzyme from doing its job, Thus the net rate of reaction observed isa balance dependent on how resistant the ‘enzyme isto heat. Enaymesin mashes such as ‘e-amylase and peroxidase are very resistant to heat, whereas others lke P-glucanase and B ‘amylase are much more heat sensitive pH, too has impacts other than on the stabiliy of the enzyme. We need to remember thatthe active site comprises several amino ‘acids drawn from different parts ofthe ovorall, polypeptide (and perhaps even several polypeptides — some enzymes contain 2 or 4 ‘separate polypeptide chains and are sald to have quaternary structure). Some of these amino acids, such as glutamic acd or sino, have side chains that can become charged (soe earlier) may bo, for instance, that the enzyme uses the negative charge ofa glutamic acd resicue to bind the substrate. I that were the case, too Jou a pH, which would make the glutamic acid Uuncharged, would lead to a cessation of ‘enzymic activity. Furthermore, some substrates can exist in uncharged of charged forms and ‘may need to bein one orothor form in ordor to ‘become attracted to the enzyme. Infact mast fonzymes oporate effectively only within a narrow pH range. Most of thse of relevance in. ‘mashing happan to work bestin the pH range of ‘mashos (betwoon 6 and 6) It is not only changes in pH which can Interfere with enzyme activiy and stabil. Enzymes aro algo susceptible to inactivation by ‘other agents (inactivator). One such substance {is the copper ion (Cu®*). This snares ~SH ‘groups and screws up ireversibly those proteins that depend on ~SH groups for their function ‘Other molocules which can block enzyme activity do so reversibly (6. i you take them ‘away enzyme activity is restored) and they are known as inhibitors. Basically here are four |ypes of inhibition that we need to concem ourselves with, Remarkably, whilst they each almost certainly occur in brewery systems, thoy haven't been studied in great detail on an tenzymme by enzyme cas. ‘The fst, competitive intibiton, results when @ molecule is so similar to the substrate ‘molecule that it can recognise” the active site and bind to it, but 1s nonetheless sufficiently ditferont that it just sits there and can't be tackled by the enzyme. It gots in the way of the Fig? A model for iso-c- acid ~ metal ion ~ protein interaction in foam. Te iso-@-acids are ‘extremely stylised, depicting only two of ther thre hydrophobic arms (=), how these hydrophobic arms interact with hydrophobic regions in polypeptides and how the negative charges in adjacent iso-cracids are neutralised ‘by bridging through a divalent metal cation (such as magnesium, manganese or zinc)..0 this way large complexes between separate ‘proteins and iso-ccacids are formed and strength is imparted to bubble walls substrate. However ifthe substrate concen: tration is high enough then it will squeeze out the inhibitor and inhibition is overcome. In non-competitive inhibition the inhibitor binds to a site an the enzyme that is not the: active sitoand,n so doing distorts the shape of the molecule so that tho active site is no longer ‘available to substrate. Removing tho inhibitor ‘lows the enzyme to side back into shape, but in this case increasing the substrate ‘concentration cannat squeeze out the inhibitor. [Atvery high substrate concentrations we can ‘sometimes ancounter substrate inhibition. Once ‘again we can turn to a football stadium for an analogy: f the crowd is dense outside and not forming an ordory lin but rather jockeying to ‘98 through a single turnstile then nobody wil enter comfortably. So it is with substrate intibiion: separate substrate molaculos interfere with one another's abilty to bind tothe active st. The fourth significant type is product Inhibition. inthis case itis departing product ‘molecules that interfere with the substrate's ably to bind ~ rtharas ita single turnstile was, being used to let people leave the stadium as. wall as bring them in, Interactions of proteins with other molecules ‘So we see thatitis not only substrate molecules that can interact wih proteins. Let's take two ‘oxamples rlovant to the brewer. ‘The fist interaction ie between the bittor ‘compounds (iso-c-aciés) and polypeptides. Former colleagues of mine, Paul Hughes and Bill Simpson proposed that the interactions involved here are o atleast two typas (Fig 7). In the first place the hydrocarbon hydrophobic, paris of the iso-cacids and those of polypeptide link. In turn the negative charges ‘on adjacent iso-a-acids are bridged by te two positive charges on a metal fon such as magnesium. Qeoves tm De et Fig 8 A model for polyphenol-protein interactions in has ‘The network formed stabilses proteins in bbubbie walls (10. in oar), Phiip Slack and had ‘alraady shown that it was those proteins which ‘are relatively hydrophobic that tend to give more stable foams. From understanding the rudiments of protein structure (as we have explored hore) we can explain why: hydrophobic groups want to get together and ‘get avay from water. (in realy its because the hydrogen-bonding wator fraternity excludes: them.) They associate together (and with other thydrephablc molecules such asthe biter acids) ‘and wl migrate to surfaces away trom the body ‘ofthe wate (or beer}. to the bubble wal. ‘The second interaction is between proteins and polyphenols. Kari Siobert found that the lati tanning moleculos have a shape that fis comfartbly with proline (see Fig 1) and that haze-forming polypeptides are rich in proline. Furthermore they ypothesised that each polyphenol ean bind to moro than a single polypeptide. Those interactions build up and bull up until large networks are produced that ‘are so big that they are no longer soluble (Fig) The result? Haze. In turn sillca hydrogol Is effective in removing haze proteins and poly: Vinylpolypyrlidone in removing polyphenols because thoy have surfaces which are siilarto, polyphenols and proline-rich proteine respectively. Solubility ‘As we have seen, the dolicate structure of proteins that presents a hydrophilic exterior with the hydrophobic groups on the inside ensures ‘soluilty buts easily cisruptod. One of tho main factors in brewing that wil do this is heat ‘Thermal nergy "blows" the structure wide ‘pan, the water hating interior is exposed and ‘those hydrophobic regions search one another ‘outwith the formation of insoluble clumps. This Is what happens in wort boing. Similarly proteins are sonsive to cold ~ the molecules Tearrange and become insoluble (cf. ching botorefitering). ‘Another agent that can come to bear is oxygen. Gerald Muts working at Heineken showed that adjacent -SH groups on proteins in ‘a mash can be oxidised to form bridges: “SH+-SH+O2 be -S-S-+H:02 In this way separate protein molecules can Join together and reach a size that makes them {ngoluble In fact in a mash this typeof reaction Contributes to tha formation of teig and the Impeding of wort flow in lautering. The more ‘oxygen present, the greater the opportunity fort tohappen. The BREWER hiteraonl + wnwighonesk roo ayFig 6 The concept of “active site inoreasing heat will also tend to disrupt the enzyme structure, deform the active site and ‘therefore prevent the enzyme from doing ts jb. Thus the net rate of reaction obsorvad is a balance dependent on how resistant the ‘enzyme isto heat. Enzymes in mashes such as ‘e-amylase and peroxidase are very resistant to heat, whoreas othorsliko B-alucanase and B amylase are much more heat sensitive PH, too has Impacts other than on the stability of the enzyme. We need to remember that the active site comprises several amino acids draven from diffrent parts of tho ovoral polypeptide (and perraps even several polypeptides — some enzymes contain 2 or 4 ‘separate polypeptide chains and are said to have quatemary structure). Some of these ‘amino acids, such as glutamic acid or lysine, have side chains that can become charged (see carter) Ttmay be for nstance, thatthe enzyme uses the negative charge ofa glutamic acid residue to bind the substrate. I that were the case, too low a pH, which would make the glutamic aia uncharged, would lead to a cessation of ‘enzymic atity. Furthermore, some substrates can exist In uncharged or charged forms and may nged tobe in one or other form in order to become attracted tothe enzyme, In fact most enzymes operate tfecvely only within a narrow pH range. Most of those of relevance in ‘mashing happen to work best nthe pH range of ‘mashes (oetween and 6) itis not only changes in pH which can interfere with enzyme activity and stabiiy Enzymes are also susceptible to inactivation by ‘other agents (inactvatrs) One such substance is the copper ion (Cu). This snares ~SH groups and screws up irreversibly those proteins that depend on ~SH groups for thei function (thor molecules which can block enzyme ctvity do so reversibly (i. if you take them away enzyme actvly is restored) and they are kaown as inhibitors. Basically there are four types of inhibition that we need to concern ourselves with. Remarkably, whilst they each ‘almost certainly occur in browery systems, thoy haven't been studied in great detail on an enzyme by enzyme case, ‘The firs, competitive inhibition, results when a molecule Is so similar 1o the substrate ‘molecule that it can “recognise” the active site and bind toi, but is nonethelass sulficiently diferent that ft just sits there and can't be tackled by the enzyme. It gets nthe way of the j Fig 7 A mode for iso-c-actd — metal ion ~ ‘vote interaction in foam. The iso-ovacids are ‘extremely stylised, depicting only woof their three hydrophobic arms (=e), how these ydrophobie arms interact with htrophobic regions in polypeprides and how the negative ‘charges in adjacent iso-ccacids are neutralised by bridging through a divalent metal cation (such as magnesium, manganese or zinc)..n this way large complexes between separate ‘proteins and iso-ac-acids are formed and strength is imparted to bubble walls substrate. Howaver i the substrate concen tration is high enough then it will squeeze out the inibtor and inhibition is overcome, In non-competitive inhibition the inhibitor binds to site on the enzyme that is not the active site and, nso doing, distorts the shape of the molecule so that the active site is no longer available to substrate, Removing the inhibitor allows the enzyme to side back into shape, but in this case increasing the substrate ‘concentration cannat squeeze out the inhibitor. ‘Atory high substrato concontrations wo can sometimes encounter substrate inhition. Once again we can turn to football stadium for an analogy I the crowd is dense outside and not forming an orderly fine but rather jockeying to {get through a single turnstile then nobody wil, ‘enter comfortably. So it is with substrate inhibin: separate substrate molecules interfere with one another's ably to bind tothe active ste ‘The fourth significant typa is product Inhibition. In ths case itis departing product molecules that interlee with the substrate’s ably to bind — rather as fa single turnstile was being used to let people leave the stadium as well as bring them in Interactions of proteins with other molecules ‘Sowe see that tis not ony substrate molecules, that can interact with proteins. Let's take two ‘examples relevant to the browor. ‘The fist interaction ie between the bitter ‘compounds (iso-c-acids) and polypeptides. Former colleagues of mine, Paul Hughes and Bill Simpson proposed that the interactions Involved hare are of at east two types (Fig 7). In the first place the hydrocarbon hydrophobic, parts of the Iso-aacids and those of polypepties link. n turn the negatve charges. ‘on adjacent iso-a-acids are bridged by the two positive charges on @ metal ion such as ‘magnesium. A trim Fig 8 A mode for polyphenol-protein interactions in haze The network formed stablises proteins in bubble walls (ein foam) Philp Slack and nad ‘aleeady shown that it was thoes proteins which are relatively hydrophobic that tend to give more stable foams, From understanding the rudiments of protein structure (as we have explored here) we can explain why: hydrophobic groups want to get together and got away from water. (in realy its bocause the hydrogen-bonding water fraternity excludes them.) They associate together (and with other yerephobic molecules such asthe ber acids) ‘and will migrate to surfaces away from the body cf the water (or beer). othe bubble walls. ‘The second interaction is between proteins ‘and polyphenols. Karl Siebort found that tho latter tanning molecules have a shape that ts comfortably with proine (see Fig 1) and that hhaze-forming polypeptides are rch in prone. Furthermore they hypothesised that each polyphenol can bind to more than a single polypeptide. These interactions build up and build up unt large networks are produced that ‘are 0 big that thay are no longar soluble (Fig) ‘The result? Haze. In turn silica hydrogel is effective in removing haze proteins and poly: Vinyipolypyroidone in removing polyphenols because they have surfaces which are similar to Polyphenols and proline-rich proteins respectively. Solubility ‘As we have seen, the delicate structure of proteins that presents a hydrophilic exterior wih the hydrophobic groups on the inside ensures solubility butis easily dsrupted. One of the main factors in brewing that wil do this is heat Thermal energy “blows” the structure wide ‘open, the water ting interior is exposed and these hydrophobic regions search one another ‘out withthe formation of insoluble clumps. This is what happons in wort boling. Similarly Proteins are sensitive to cold — the molecules Fearrange and become Insoluble (e1. ehiling boforefitering. ‘notes agent that can come to bear is oxygen, Gerald Muts working at Heineken showed that adjacent -SH groups on proteins in ‘a mash can be oxidised to form bridges: ‘SH 4:SH+ Op > -S-S-+Ha02 In this way separate protein molecules can Join together and reach a size that makes them Ingoluble In fact a a mash this type of reaction Contributes to the formation of fag and the impeding of wort flow in lautering, The more ‘oxygon present, the grater the opportunity fort tohappen. The BREWER nero!» worihorguk + March 2001Atoms The basic unit of all matter is the atom. Modern thinking about the atom is all about waveforms, but it is still convenient to talk about the terms of protons, neutrons and electrons. © {Atthe hoart ofthe atom (the nucteus) are the protons and neutrons, each of which has a ‘mass of one. Protons are positively charged, neutrons have no charge. Together they ‘comprise the mass of the atom, ‘tbiting the nucleus, rather like the planets ‘orbit the sun, are electrons. They are negatively charged, but have essentially no mass. In neutral atoms the number of ‘lzctrons is exactly the same as the number of protons. ‘The electrons orbit the nucleus in defined orbits. There is a imi to how many electrons ‘can occupy each orbit. The orbit nearest to the nucleus can accommodate just two lactrons. Because they are so close to the ‘ucleus, the strong posive-negative interaction means that these electrons are less fe to move around than those further out i.0. they have a relatively iow energy. The next orbit holds eight electrons, which because they are that much further away are more energetic. Tho next orbit holds 18, then the next one 82..and 8000, Each ofthe eloments in nature consists of atoms. There are well over one hundred ‘elements, each of them having successively fone extra proton and thorafore one extra lactron. The simplest, hydrogen, has one proton and one electton. The next is helium: it hhas two protons (and also two neutrons, soit hhas a mass of 4 and not 2) and 2 electrons and 80 on. ‘The most stable (least reactive elements) are those inwhich the outermost orbits upto ‘capacity with electrons (2,8, 18 et). Helium, then, is very unreactive and thats why we ‘can be rather more comfortable tng in FACTFILE - some necessary chemistry “March 2001+ The BREWER Ierotina » wworigharg ak ‘alhips files with helium as opposed to hydrogen. ‘One way in which an atom can complete its ‘outer shel of eloctrons is by donating flectrons to another atom which inturn can complete is outer orbit by accepting electrons. For example sodium (which has one electron Ins outer orbital) can ose @ single electron ‘and chiorine (which has seven electrons in ts cuter orbital) can gain an electron, each then ‘assuming fll outar orbits Sodium aoquires & net charge of 1* because ithas lost one slecron, chloride gains a net charge of 1, cause It has one extra electron. The ‘compound formed is NaCl. The sodium has become a positively charged ion, somatimes called. cation because itis atracted oa negatively charged electrode (the cathode) Chioride has become a negatively charged ion (an anion), Magnesium needs to lose two electrons, ‘which i ean by donating one electron to each ‘of two chlorings. Thus magnesium chloride consists of one magnesium and two Chlorides, MgCl, This type of bond is called {an jonie bon. ‘Alternatively an atom can complet is otbilal by sharing electrons. Thus i the orbitals of two hydrogen atoms (one electron each) come into contact with the outer orbital cof an oxygen atom (sx electrons) thon a palt of electrons can be shared between the ‘oxygen and each hydrogen atom to make a much mote stable molecule, water, 20, Tris {ype of bonding is called a ‘covalant bond! ‘The numberof other atoms that an olemont ‘can reac with is known as its valence’. Thus hydrogen reacts with only one atom at atime, valence = one; oxygen reacts with two to ‘make it more stable, valence = two, Ergo we have water with two atoms of hydrogen and ‘ono of oxygen, H:O. Carbon has a valence of four. Sometimes one atom i inked to another by two links ~ ths is called a ‘double bond? and tis stronger than a single bond. An atom ‘can use up two o its valences inthis way ‘Thus in carbon dioxide, COp, the carbon uses up ts fourvalencos by inking to two oxygons by double bonds, with each oxygen using up its two valences in a double bond to the carbon 0=-0 Oxidation and reduction |Woxygen is added toa substance then that substance is sad to be oxidised. Conversoly it hydeogon is adds its said to be reduced. Equally, removal of hydrogen is alsa ‘dation. I you wil allow one jump of logic without elaborate explanation, when a substance loses electrons, iti also ssid to have been oxidised. The substance that picks up those electrons is said to be reduced. This is one type of chemical reaction. An ‘example is the conversion of acetaldehyde to ethanol by yeast. Acetaldehydeis reduced, land the molecule NADH, which isthe Substance ining organisms which cares the elestrons (reducing power), has become oxidised. one component ofa system is oxidised, another component or components ‘must be reduced. The reducing power balances: CCHSCHO + NADH + H* 49 CHaCH:OH + NAD. Acelaldehyde| Ethanol Reactions ‘All chemical reactions also balance: the total numberof atoms of given element on the loft sido ora reaction must balanco with that ‘nthe right. An exampla would be the ‘conversion of glucose to ethanol and carbon indicatas that the reactions raversiole (can move in bath directions). the pH is low (high H® concentration) ther this ‘wl tend to push the reaction towards the lot tthe pH is high (ow H* concentration) then. ‘the reaction wil end to move towards the right, in order to produce more HY. ‘The amino group can pick up a hydrogen Jon ands sald to be baste, Anather basa Is the hydroxide ton, OFF -NHe + HY > NHst OW+H* © 120 ‘The measure of acidity is the pH scale. pH log 1H" ‘The scale runs from 1 (extremely acidic) to 14 (oxtromoly basic), with 7.0 being neutral. Mey Dent) ee enact Ped Polymers are very large molecules in ee eer eet re aoe Pes Morera ocd Cee etd Se eae es aca os Petree aa mes oe morcig Nea uate) ‘on. Short chains of perhaps 2 to 10 ec) eee eS eee re (© 4 BREWER'S BIOCHEMISTRY. Inthe May edition of The Brower International, Protessor Bamtorth Continues with Polysaccharides. In July he will discuss Lipids, followed by 'Nuclole acids and Metabolism in September and November respectively. TheBRI ‘This page could be your ad in the next edition of The Brewer International Maximise your advertising budget by making The Brewer International your first choice. Call our agents ‘The Carling Partnership for full details. +44 (0) 20 7404 6999 F: +44 (0) 20 7831 4995, E-Mail: enquiries@igb.org.uk The BREWER International B atin» woop + March 201