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MALT PEPTIDASES
Author(s) -
Jones Margaret,
Pierce John S.
Publication year - 1967
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1967.tb03053.x
Subject(s) - mashing , hydrolysis , chemistry , amino acid , trypsin , lysine , biochemistry , enzyme , arginine , proline , thiol
Malt contains some peptidases which are inactivated by oxidation of the thiol groups in their molecules but only slightly activated by reducing agents. Peptidases with a trypsin type of specificity, restricted to the hydrolysis of basic bonds linking carbonyl groups of arginine or lysine to the amino groups of other amino acids, do not appear to be significantly active under the defined brewery mashing conditions. There is evidence that some proline is produced by an enzyme system different from that producing other amino acids.