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Influence of carboxypeptidases on free amino acid, peptide and methylpyrazine contents of under‐fermented cocoa beans
Author(s) -
Yusep I,
Jinap S,
Jamilah B,
Nazamid S
Publication year - 2002
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1232
Subject(s) - carboxypeptidase , carboxypeptidase a , isoleucine , chemistry , leucine , valine , biochemistry , phenylalanine , amino acid , food science , fermentation , exopeptidase , alanine , enzyme
A study of the action of two carboxypeptidases on free amino acids, peptides and methylpyrazines in under‐fermented cocoa beans was carried out. Carboxypeptidase B from porcine pancreas and carboxypeptidase Y from baker's yeast were used separately for digestion. Hydrophobic free amino acids (alanine, valine, isoleucine, leucine, phenylalanine and tyrosine) were predominantly produced in samples digested with both carboxypeptidase B and Y. The peptide patterns of samples digested with both carboxypeptidases were similar to that of the control. The concentration of 2,3,5,6‐tetramethylpyrazine in samples with carboxypeptidase B addition was significantly higher than those of 2,5‐dimethyl‐ and 2,3,5‐trimethylpyrazine; the concentration of 2,3,5‐trimethylpyrazine was highest (1727.86 µg per 100 g) in the sample with carboxypeptidase B addition that had been incubated for 24 h. These findings indicate that carboxypeptidase B from porcine pancreas was more prominent in the formation of cocoa‐specific aroma. © 2002 Society of Chemical Industry