Enzymes

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An enzyme is a protein that facilitates a chemical reaction. Enzymes play an important role in every fermented beverage.

For beer production, grain is malted in order to increase the amount of enzymes. Enzymes active during the mash include α- and β-amylase, proteases, peptidases, β- (1,3)(1,4)-glucanases and lipases.[1] The most important action of these enzymes is that during the mash they break down the starches in the grain into fermentable sugars. Brewers may sometimes add extra enzymes such as glucoamylase in order to further break down the complex sugars (dextrins). Hops also have enzymes that can break down dextrins.

Proteolytic enzymes in the mash and their optimal temperatures:[2]

  • Endopeptidases (45-50°C)
  • Carboxypeptidase (50°C)
  • Aminopeptidase (45°C)
  • Dipeptidases (45°C)


Even the complete removal of oxygen would not be able to prevent oxidation of fatty acids by lipoxygenases (LOX). These enzymes are formed during malting and activated during milling. Enzyme active is enhanced with a low dough-in temperature and pH closer to 6.0.[2]

In wine production, a group of enzymes known as pectinase is commonly added to improve clarity and extraction.

Microbes use a large variety of enzymes in order to grow, survive, and conduct fermentation. (See Fermentation.)

Some enzymes can have a negative impact (such as polyphenol oxidase in fruit) and we can take steps to inhibit their undesirable effects.

The action of enzymes is influenced by pH, temperature, and other factors. High temperatures will permanently disable enzymes because the protein structure becomes irreversibly distorted, preventing them from functioning.

References

  1. Szwajgier, D. "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. vol. 117, no. 4, 2011, pp. 569–577.
  2. a b Kunze, Wolfgang. "3.2 Mashing." Technology Brewing & Malting. Edited by Olaf Hendel, 6th English Edition ed., VBL Berlin, 2019. p. 230.