Proteins and Enzymes PDF

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 ↳ !nsa etmek   α - α α -  # α - - α -  - - - #You don't need to draw but you need to recogn!ze them  need to take w!th * Prote!ns structure are more complex than hydrocarbons you ↑ food nonpolar nonpolar nonpolar electr!cally nonpolar nonpolar charged electr!cally charged polar nonpolar  *  Y hemoglob!n - - - * propert!es of prote!n - - -  - - - - - - -- - ↓ measure am!no ac!d  Amino acids can be separated by ion exchange chromatography or reverse phase HPLC. HPLC is an abbreviation for High-Performance Liquid Chromatography. Among the various technologies developed for chromatography, devices dedicated for molecular separation called columns and high-performance pumps for delivering solvent at a stable flow rate are some of the key components of chromatographs. Ion chromatography is a form of chromatography that separates ions and ionizable polar molecules based on their affinity to the ion exchanger. Dansylchloride, Edman’s reagent (UV detection) oro-phthalaldehyde + mercaptoethanol (fluorescent) are used for quantification.  50'den fazla aa'lar (d!z!ler!) !c!n kullanlmaz. ↳ Edman degradat!on  l!ke sphere globular prote!n + struct. * tw!sted form 2-hel!x form ↑ TLCMS > measure - aa compos!t!on denature. not structure shows whether the prote!n or * Secondry * Denaturat!on = unfold!ng the prote!n pept!des (1. yapls! deg!l , 2., 3. ve 4. yaplarnn bozulmasyla our. * Dur!ng cheese mak!ng+ denaturat!on of prote!ns (kem!k suyunun katlasnca jel!ms! olmasl) # Collagen denaturat!on- convert gelat!n # * C-hel!x veya B-hel!x yaplarnn deg!mes! denaturat!on g!ster!r. ⑪ olur. * Ethanol b!r solvent de prote!n!n !s denges!n! bozduyu !s!n denaturat!ona sebep veya baska Aa Bu da prote!n denature our !yon!zasyonu deg!s!rse , yuk denges! de!z!r 3 4 etk!ler ve * ve yaplyl...... denature faktorlerden b!r!d!r Ga'ler!n olur. * ph prote!n! eden. !yon!zasyonuna sebap yn sek!lde tuz da  * non-covalent hydrogen bond!ng - - β *  α α α - α β α β * three d!mens!onal arrangement her!agroups s R The overall three-dimensional arrangement of all atoms in a protein is referred to as the protein’s tertiary structure. The mature, stable structure of a single peptide sequence Tertiary - structure includes longer-range interactions of amino acid sequence. Formed and maintained by interactions among R groups for the amino acids in the protein. These interactions allow the peptide chain with its secondary structure to fold further on itself, forming compact spherical structures. 4 factors are responsible for tertiary structures of proteins : →Disulfide linkages →Hydrogen Bonding →Electrostatic interactions →Hydrophobic interactions I kal!nt! aras !nd a X x - - - - -  b!nd!ng of several polypept!des Khemoglob!n -  β > - we!ght prote!n 1% 80 lactoglobul!n !n we!ghte) salts & some protect denaturat!on aga!nst - Ikorur) Idenaturat!on s!cakl!gn!n ortmas) - * some salts cause d!srupt H bonds !n secondary denaturat!on (denaturasyou > - structure s!cakl!gn!n azalmas) - - (denaturasyona) sebep ou ↑ m!dahale etmek -  alter = dej!st!rmek d!ser Su tutma kapas!tes! most plant prote!ns not soluble !n neutral pH. we * are try!ng to mod!f!ed prote!n to soluble !n neutral pH.. T↑ solub!l!ty ↑ shake ,z!nmes! !s!n. * we!ght prote!n yapl!r If the prote!n make good hydrogen bonds w!th water. > - # Solub!l!ty - !mportant for prote!n f!rst th!ng !s check the t when you produce prote!n source , solub!l!ty of the prote!n * denaturat!on -> decrease solub!l!ty  & bell! * solub!l!ty test ; prote!n powder , b!r haz!rlanan solut!on !c!ne pH'ta al!np !ncelen!r. koyulur ve koken kusm L!v!nde ne kadar prote!n Gokmes parabol!c vs. d!ye #I + !solectr!c po!nt , prote!n !n d!sk solub!l!ty olduu pH nok- enas!na den!r. * m!n repuls!on , max attract!on. Ben - * At lower pH w!ll dom!nate X aa groups , at H!gh PH , hydrocarbons w!ll they cause repuls!on , and !t !ncrease solub!l!ty. dom!nate , !t , !ncrease solub!ty  4 tad de!st!reb!l!r - conta!n (-SH) Y !l! SH olmasI texture etk!ler > - - NH2 (a a). , reduc!ng sugar  * Et mar!nasyonu + prote!n hydrolys!s Et! !nc!rle beklet!rsek lokum olur G!nkl * ananas veya g!b! yumusar ananas ve !nc!-. , r!n !g!nde proteases enz!m! var ve et!n !g!ndek! prote!nler! h!dro l!z eder Fakat. tad!n de!st!rmez , G!nk! a a'lar deg!l prote!nler! h!drol!z eder. k!kab!l!r. * Glycat!on - : to mod!f!ed prote!n/sugar ↓ attached prote!n I ekleyerekzell!kler!n! B!r prote!n! parcalamadan , seker de!st!rmek ( allulose : rare sugar  # (Techno Funct!onal) ⑭ E k!kab!l!r #a * H20 b!nd!ng * o!l b!nd!ng Agelat!on ksolub!l!ty * emuls!f!cat!on #Foam!ng  - - - - - -- > hydrodynam!c -    - Mercu -- --- - -  - - - -  * B!r prote!n!n balamas ayn anda yaj balama ve su yuksek olab!l!r Inonpolar veya polar olduunu gastermez , prote!n porelarna da yaj dolmus olab!l!r) !ncrease as TX A bond!ng t > - , -  -  #wheat elast!c structure + g!ves - - > > - gluten prov!des -  ten!n -> gluten ad!n & - - water-!nsoluble T - https://www.sciencedirect.com/science/article/pii/B012227080001714 6 leaven!ng + mayalama 4 gas format!on - the yeast - produce CO2 texpand dough tr!se Isolub!l!ty  b!olog!cal bak!ng powder - 202 + chem!cal leaven!ng leaven!ng * CO2 & yeast + + * gluten-free flavor + conta!n d!fferent polysaccar!des - psyll!um, zac!tan etc. ↳th!s prov!de - or!g!nal - volume asInten bread g - preserve extens!on bran layer -> + for tam buday ekmej! - * m!s!r ekme! s!kl!k yap' - no gluten > - but excess consum!ngoner!lmez.  and #h!gh prote!n - unbleached a bread flavor a more elast!c b!gger * low prote!n + bleached + cake flavor + less elast!c and smaller - less gluten > - but more starch- removed the Stach & gluten-free bread top , n!ce , plant products (soy bean ↓ small volume back Wheat (Kara bugday) , qu!ne a very Observed Ts!yez bulgur barley larpal , , , rya (avdar) ta!n gluten * cake vS bread - - 6 8% - 12-14 % + gluten color Ebleached / unbleached E decolor!zat!on z get r!d of yellow!sh ↳ weakness structure bleach!ng the gluten = ↳ best !s the use hydrogen perox!de (H2O2) way sourdough bread - saccharomyces Lact!c ac!d a cerev!s # bacter!a - -m produce some protraz > - weak the gluten structure t enzyme  # + - v!l! boyleyken d!zles!r ↳ n!ab!r say s!nd!remene  * Gluten sens!t!v!ty > - more allerg!c - not severe as cel!ac * Golyak hastal!g olmamas!na ragmen Iyan! gluten cut yap!lab!lmes!ne ragmen glutens!z beslenme sagl!kl! deg!l G!nkbayursak. floras barsak hareketler!n! azalt!r , m!crob!otaya !y! em!l!m azal!r result sens!t!v!ty gelmez ,. - may or d!sease and gluten!n non-polar R * gl!at!n conta!n group aa.  pro te!n yoghurt- gels : - cheese , Jams , - ↳ jell!es - , cold bond qu!ce, cand!es, set pudd!ng, Endegg turk!sh del!ghts , - #enature + rap #20 + ge structure !n need order to make get we polymer trap HeO - - kneed certa!n level of concentrat!on to produce get T ↳ d!spersed systems + not solved !n each other - * - * prevent phase separat!on - --  - we need th!s type - - # gas + l!qu!d-gas trapped !n l!qu!d = foam *  ↑ stab!l!ty of form ↑ prote!n ↳ less than emuls!f!er motor n!trogen Content + correct - prote!n - !nsoluble - ↳ NaOH , sulfr!k ac!d etc. more chem!cal need > - others measure soluble prote!ns collagen -+ dropz droysat gelat!n soluble ↓ heat not soluble β α MT2 sonu   Temperature pH Wateractivity IonicStrength Chemicals Chelating agents Reducing agents