Editing Enzymes
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An enzyme is a [[protein]] that catalyzes a chemical reaction, greatly speeding it up while not being consumed by the reaction. This allows enzymes to be active even in very low concentrations. Enzymes play an important role in the creation of all fermented beverages, and more generally, they are needed for all life processes.<ref name=kunzemashing/> As with all proteins, enzymes have particular temperature and pH ranges in which they function, and more narrow ranges in which the activity is considered optimal. | An enzyme is a [[protein]] that catalyzes a chemical reaction, greatly speeding it up while not being consumed by the reaction. This allows enzymes to be active even in very low concentrations. Enzymes play an important role in the creation of all fermented beverages, and more generally, they are needed for all life processes.<ref name=kunzemashing/> As with all proteins, enzymes have particular temperature and pH ranges in which they function, and more narrow ranges in which the activity is considered optimal. The effect of temperature is greater than the effect of pH. Knowing the optimal ranges can be helpful, but it must be realized that the enzymes will be active to some extent outside those ranges.<ref name=bsp/> Enzymes denature (the three-dimensional structure unfolds) at higher temperatures, rendering them inactive.<ref name=kunzemashing/> Enzymes tend to have a very specific substrate upon which they act, and therefore are often named after the substrate, adding "-ase" to the end.<ref name=fix>Fix G. [[Library|''Principles of Brewing Science.'']] 2nd ed. Brewers Publications; 1999.</ref> | ||
'''Coenzymes''': The action of many enzymes is tied to the presence of an additional non-protein component that binds with its structure. For example, bivalent metal ions (e.g. iron, magnesium, calcium) are often involved as coenzymes.<ref>Kunze, Wolfgang. ''Technology Brewing & Malting.'' Edited by Olaf Hendel, 6th English Ed., | '''Coenzymes''': The action of many enzymes is tied to the presence of an additional non-protein component that binds with its structure. For example, bivalent metal ions (e.g. iron, magnesium, calcium) are often involved as coenzymes.<ref>Kunze, Wolfgang. ''Technology Brewing & Malting.'' Edited by Olaf Hendel, 6th English Ed., VBL Berlin, 2019. p. 54.</ref> | ||
'''Isoenzymes''': Enzymes that have different structures but catalyze the same reaction are called isoenzymes. Each isoenzyme may have different characteristics such as optimal temperature and pH ranges. Generally, most enzymes in living organisms have several isoenzymes. | '''Isoenzymes''': Enzymes that have different structures but catalyze the same reaction are called isoenzymes. Each isoenzyme may have different characteristics such as optimal temperature and pH ranges. Generally, most enzymes in living organisms have several isoenzymes. | ||
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** '''Cytase''' degrades cell wall structures.<ref name=fix/> | ** '''Cytase''' degrades cell wall structures.<ref name=fix/> | ||
=== Mashing === | ===Mashing=== | ||
During [[mashing]], a very large number of enzymes act simultaneously on the components of the grist under conditions that are far from optimal for many of them in terms of substrate concentration and accessibility, pH, and enzyme stability. Enzymes are progressively inactivated at different rates depending on the temperature, the pH, the presence of substrate and other substances (such as tannins and cofactors such as calcium ions) in solution.<ref name=bsp/> Starch, proteins, nucleic acids, lipids and other substances are degraded, usually by hydrolytic (cleaving) reactions, but other reactions, such as oxidations, also occur.<ref>Szwajgier D. [https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.2050-0416.2011.tb00505.x Dry and wet milling of malt. A preliminary study comparing fermentable sugar, total protein, total phenolics and the ferulic acid content in non-hopped worts.] ''J Inst Brew.'' 2011;117(4):569–577.</ref> | During [[mashing]], a very large number of enzymes act simultaneously on the components of the grist under conditions that are far from optimal for many of them in terms of substrate concentration and accessibility, pH, and enzyme stability. Enzymes are progressively inactivated at different rates depending on the temperature, the pH, the presence of substrate and other substances (such as tannins and cofactors such as calcium ions) in solution.<ref name=bsp/> Starch, proteins, nucleic acids, lipids and other substances are degraded, usually by hydrolytic (cleaving) reactions, but other reactions, such as oxidations, also occur.<ref>Szwajgier D. [https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.2050-0416.2011.tb00505.x Dry and wet milling of malt. A preliminary study comparing fermentable sugar, total protein, total phenolics and the ferulic acid content in non-hopped worts.] ''J Inst Brew.'' 2011;117(4):569–577.</ref> | ||
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* Protein degradation and oxidation (see [[Protein]]) | * Protein degradation and oxidation (see [[Protein]]) | ||
** '''Endopeptidases''', which include '''metalloproteases''', '''cysteine proteases''', '''aspartic proteases''', and '''serine proteases''' (optimal 45–50°C, pH 3.9–5.5) over 40 different endopeptidase enzymes degrade proteins into peptides and free amino acids.<ref name=esslinger/><ref name=kunzemashing>Kunze W. Wort production. In: Hendel O, ed. [[Library|''Technology Brewing & Malting.'']] 6th ed. | ** '''Endopeptidases''', which include '''metalloproteases''', '''cysteine proteases''', '''aspartic proteases''', and '''serine proteases''' (optimal 45–50°C, pH 3.9–5.5) over 40 different endopeptidase enzymes degrade proteins into peptides and free amino acids.<ref name=esslinger/><ref name=kunzemashing>Kunze W. Wort production. In: Hendel O, ed. [[Library|''Technology Brewing & Malting.'']] 6th ed. VBL Berlin; 2019. p. 230.</ref> | ||
** '''Carboxypeptidases''' (optimal 50°C, pH 4.8–5.6) degrade proteins & peptides into free amino acids.<ref name=esslinger/><ref name=kunzemashing/> | ** '''Carboxypeptidases''' (optimal 50°C, pH 4.8–5.6) degrade proteins & peptides into free amino acids.<ref name=esslinger/><ref name=kunzemashing/> | ||
** '''Aminopeptidases''' (optimal 45°C, pH 7.0–7.2) degrade proteins & peptides into free amino acids.<ref name=esslinger/><ref name=kunzemashing/> Inactive during mashing. | ** '''Aminopeptidases''' (optimal 45°C, pH 7.0–7.2) degrade proteins & peptides into free amino acids.<ref name=esslinger/><ref name=kunzemashing/> Inactive during mashing. | ||
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* Phenolic compound release or oxidation (see [[Phenolic compounds]], [[Oxidation]]) | * Phenolic compound release or oxidation (see [[Phenolic compounds]], [[Oxidation]]) | ||
** '''Polyphenol oxidase''' (optimal 60–65°C, pH 6.5–7.0) oxidizes polyphenols, especially lower molecular weight polyphenols (e.g. catechin).<ref name=esslinger/><ref name=quibai>Quinde-Axtell Z, Baik BK. [https://pubs.acs.org/doi/abs/10.1021/jf060974w Phenolic compounds of barley grain and their implication in food product discoloration.] ''J Agric Food Chem.'' 2006;54(26):9978–9984.</ref><ref name=quipow>Quinde-Axtell Z, Powers J. Baik BK. [https://onlinelibrary.wiley.com/doi/abs/10.1094/CC-83-0385 Retardation of discoloration in barley flour gel and dough.] ''Cereal Chem.'' 2006;83(4):385–390.</ref><ref name=adb/> Polyphenol oxidase loses activity during malting, being largely destroyed by kilning (although still active in pils malt), and it may be entirely destroyed depending on the temperature (even in pale malt).<ref name=clalar | ** '''Polyphenol oxidase''' (optimal 60–65°C, pH 6.5–7.0) oxidizes polyphenols, especially lower molecular weight polyphenols (e.g. catechin).<ref name=esslinger/><ref name=quibai>Quinde-Axtell Z, Baik BK. [https://pubs.acs.org/doi/abs/10.1021/jf060974w Phenolic compounds of barley grain and their implication in food product discoloration.] ''J Agric Food Chem.'' 2006;54(26):9978–9984.</ref><ref name=quipow>Quinde-Axtell Z, Powers J. Baik BK. [https://onlinelibrary.wiley.com/doi/abs/10.1094/CC-83-0385 Retardation of discoloration in barley flour gel and dough.] ''Cereal Chem.'' 2006;83(4):385–390.</ref><ref name=adb/> Polyphenol oxidase loses activity during malting, being largely destroyed by kilning (although still active in pils malt), and it may be entirely destroyed depending on the temperature (even in pale malt).<ref name=clalar/> Polyphenol oxidase is able to catalyze the oxidation of polyphenol compounds with oxygen into very reactive quinonic compounds.<ref name=cargon/> Polyphenol oxidase is the main responsible for the enzymatic browning in fruits and vegetables.<ref name=cargon/> | ||
** '''Feruloyl esterase''' AKA '''ferulic acid esterase''' AKA '''cinnamoyl esterase''' (optimal activity 40–50°C, pH 5.2–6.6) liberates phenolic acids (mainly [[ferulic acid]]) from [[beta-glucans and arabinoxylans|arabinoxylans]].<ref name=adb/><ref name=schwarz>Schwarz KJ, Boitz LI, Methner FJ. [https://www.tandfonline.com/doi/abs/10.1094/ASBCJ-2012-1011-02 Release of phenolic acids and amino acids during mashing dependent on temperature, pH, time, and raw materials.] ''J Am Soc Brew Chem.'' 2012;70(4):290–295.</ref> Inactive at 65°C and above.<ref name=wangas>Wannenmacher J, Gastl M, Becker T. [https://ift.onlinelibrary.wiley.com/doi/abs/10.1111/1541-4337.12352 Phenolic substances in beer: Structural diversity, reactive potential and relevance for brewing process and beer quality.] ''Compr Rev Food Sci Food Saf.'' 2018;17(4):953–988.</ref> | ** '''Feruloyl esterase''' AKA '''ferulic acid esterase''' AKA '''cinnamoyl esterase''' (optimal activity 40–50°C, pH 5.2–6.6) liberates phenolic acids (mainly [[ferulic acid]]) from [[beta-glucans and arabinoxylans|arabinoxylans]].<ref name=adb/><ref name=schwarz>Schwarz KJ, Boitz LI, Methner FJ. [https://www.tandfonline.com/doi/abs/10.1094/ASBCJ-2012-1011-02 Release of phenolic acids and amino acids during mashing dependent on temperature, pH, time, and raw materials.] ''J Am Soc Brew Chem.'' 2012;70(4):290–295.</ref> Inactive at 65°C and above.<ref name=wangas>Wannenmacher J, Gastl M, Becker T. [https://ift.onlinelibrary.wiley.com/doi/abs/10.1111/1541-4337.12352 Phenolic substances in beer: Structural diversity, reactive potential and relevance for brewing process and beer quality.] ''Compr Rev Food Sci Food Saf.'' 2018;17(4):953–988.</ref> | ||
** '''β(1-4)-endoxylanase''' releases xylooligosaccharides<ref name=schwarz/> | ** '''β(1-4)-endoxylanase''' releases xylooligosaccharides<ref name=schwarz/> | ||
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** '''Catalase''' catalyses the conversion of peroxides to water and ground state (unreactive) oxygen, however it is rapidly destroyed during mashing at 149°F (65°C) and therefore it is largely irrelevant in the brewhouse.<ref name=etokakpan/> inactivated rapidly during mashing at 65°C.<ref name=poyri>Pöyri S, Mikola M, Sontag-Strohm T, Kaukovirta-Norja A, Home S. [https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.2050-0416.2002.tb00550.x The formation and hydrolysis of barley malt gel-protein under different mashing conditions.] ''J Inst Brew.'' 2002;108(2):261–267.</ref> catalase - inactivated rapidly during mashing at 65°C.<ref name=poyri/> Catalase is denatured during mashing at 65C.<ref name=clalar/> 2H<sub>2</sub>O<sub>2</sub> --> 2 H<sub>2</sub>O + O<sub>2</sub> | ** '''Catalase''' catalyses the conversion of peroxides to water and ground state (unreactive) oxygen, however it is rapidly destroyed during mashing at 149°F (65°C) and therefore it is largely irrelevant in the brewhouse.<ref name=etokakpan/> inactivated rapidly during mashing at 65°C.<ref name=poyri>Pöyri S, Mikola M, Sontag-Strohm T, Kaukovirta-Norja A, Home S. [https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.2050-0416.2002.tb00550.x The formation and hydrolysis of barley malt gel-protein under different mashing conditions.] ''J Inst Brew.'' 2002;108(2):261–267.</ref> catalase - inactivated rapidly during mashing at 65°C.<ref name=poyri/> Catalase is denatured during mashing at 65C.<ref name=clalar/> 2H<sub>2</sub>O<sub>2</sub> --> 2 H<sub>2</sub>O + O<sub>2</sub> | ||
** '''Superoxide dismutase''' catalyses the formation of peroxides from superoxides which in the absence of catalase leads to the formation of the hydroxyl radical.<ref name=etokakpan>EtokAkpan OU. [https://link.springer.com/article/10.1023/B:WIBI.0000043169.65135.b4 Preliminary study of fat oxidation in sorghum and maize brewing.] ''World J Microbiol Biotechnol.'' 2004;20:569–573.</ref> inactivated rapidly during mashing at 65°C.<ref name=poyri/> superoxide dismutase - inactivated rapidly during mashing at 65°C.<ref name=poyri/> SOD is destroyed within 15 minutes of mashing at 65C.<ref name=clalar/> 2O<sub>2</sub><sup>-</sup> + 2H<sup>+</sup> --> O<sub>2</sub> + H<sub>2</sub>O<sub>2</sub> | ** '''Superoxide dismutase''' catalyses the formation of peroxides from superoxides which in the absence of catalase leads to the formation of the hydroxyl radical.<ref name=etokakpan>EtokAkpan OU. [https://link.springer.com/article/10.1023/B:WIBI.0000043169.65135.b4 Preliminary study of fat oxidation in sorghum and maize brewing.] ''World J Microbiol Biotechnol.'' 2004;20:569–573.</ref> inactivated rapidly during mashing at 65°C.<ref name=poyri/> superoxide dismutase - inactivated rapidly during mashing at 65°C.<ref name=poyri/> SOD is destroyed within 15 minutes of mashing at 65C.<ref name=clalar/> 2O<sub>2</sub><sup>-</sup> + 2H<sup>+</sup> --> O<sub>2</sub> + H<sub>2</sub>O<sub>2</sub> | ||
** '''Oxalate oxidase''' | ** '''Oxalate oxidase''' Active during mashing<ref name=kanbam2/> | ||
** '''Ascorbate (per)oxidase''' (optimal pH 5.5) - catalyzes the oxidation of [[ascorbic acid]] by hydrogen peroxide.<ref name=kanoxi>Kanauchi M. [https://www.intechopen.com/chapters/56077 Oxidative enzyme effects in malt for brewing.] In: Kanauchi M, ed. ''Brewing Technology.'' IntechOpen. 2017:29–47.</ref> Highly active during mashing.<ref name=kanbam2/> | ** '''Ascorbate (per)oxidase''' (optimal pH 5.5) - catalyzes the oxidation of [[ascorbic acid]] by hydrogen peroxide.<ref name=kanoxi>Kanauchi M. [https://www.intechopen.com/chapters/56077 Oxidative enzyme effects in malt for brewing.] In: Kanauchi M, ed. ''Brewing Technology.'' IntechOpen. 2017:29–47.</ref> Highly active during mashing.<ref name=kanbam2/> | ||
===Fermentation=== | ===Fermentation=== | ||
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**'''Phenylacrylic acid decarboxylase (PAD1)''' is not actually a decarboxylase, but catalyzes the synthesis of an FMN-related co-factor required for the function of FDC1<ref name=len/> | **'''Phenylacrylic acid decarboxylase (PAD1)''' is not actually a decarboxylase, but catalyzes the synthesis of an FMN-related co-factor required for the function of FDC1<ref name=len/> | ||
**'''Ferulic acid decarboxylase (FDC1)''' catalyzes the decarboxylation of cinnamic acid and derivatives.<ref name=len/> | **'''Ferulic acid decarboxylase (FDC1)''' catalyzes the decarboxylation of cinnamic acid and derivatives.<ref name=len/> | ||
===Wine=== | |||
''Coming eventually'' | |||
==Added enzymes== | ==Added enzymes== | ||
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Potential sources | Potential sources | ||
*http:// | *http://lowoxygenbrewing.com/forum/viewtopic.php?f=11&t=1821 | ||
*[http://www. | *[http://www.lowoxygenbrewing.com/wp-content/uploads/2017/04/BrewingScience_0910_James_2014.pdf Amino Acid Permeases and their Influence on Flavour Compounds in Beer] | ||
*https://scholar.google.com/scholar?hl=en&as_sdt=1%2C36&q=sun+A+quantitative+assessment+of+the+importance+of+barley+seed+alpha-amylase%2C+beta-amylase%2C+debranching+enzyme+and+alpha-glucosidase+in+starch+degradation.&btnG=#d=gs_qabs&u=%23p%3DRr5Dbt7Zj7MJ | *https://scholar.google.com/scholar?hl=en&as_sdt=1%2C36&q=sun+A+quantitative+assessment+of+the+importance+of+barley+seed+alpha-amylase%2C+beta-amylase%2C+debranching+enzyme+and+alpha-glucosidase+in+starch+degradation.&btnG=#d=gs_qabs&u=%23p%3DRr5Dbt7Zj7MJ | ||
*https://www.researchgate.net/profile/Ahmed_Gomaa35/publication/323252887_Application_of_Enzymes_in_Brewing/links/5b5f33ae458515c4b2531f59/Application-of-Enzymes-in-Brewing.pdf | *https://www.researchgate.net/profile/Ahmed_Gomaa35/publication/323252887_Application_of_Enzymes_in_Brewing/links/5b5f33ae458515c4b2531f59/Application-of-Enzymes-in-Brewing.pdf | ||
*https://hibernianbrewingschool.ie/wp-content/uploads/2015/09/The-role-of-enzymes-IOB.pdf | |||
*http://www.knudsenbeverageconsulting.com/wp-content/uploads/2011/mbaa/mbaarmdpresentationenzymesinbrewing51102.pdf | *http://www.knudsenbeverageconsulting.com/wp-content/uploads/2011/mbaa/mbaarmdpresentationenzymesinbrewing51102.pdf | ||
*http://themodernbrewhouse.com/forum/viewtopic.php?f=11&t=2168 | *http://themodernbrewhouse.com/forum/viewtopic.php?f=11&t=2168 |