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DECREASED PROTEOLYSIS OF ALKALI‐TREATED PROTEIN: CONSEQUENCES OF RACEMIZATION IN FOOD PROCESSING
Author(s) -
HAYASHI RIKIMARU,
KAMEDA IKUKO
Publication year - 1980
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1980.tb06572.x
Subject(s) - racemization , chemistry , proteolysis , casein , pepsin , residue (chemistry) , lysozyme , alkali metal , tritiated water , ribonuclease , chromatography , bovine pancreatic ribonuclease , biochemistry , food science , tritium , enzyme , organic chemistry , rna , physics , nuclear physics , gene
When proteins (pancreatic ribonuclease A, hen egg lysozyme, the acidic fraction of soybean protein, and casein) dissolved in 0.2N NaOH in tritiated water were allowed to stand at 40°C, pepsin digestiblity extensively decreased in the initial stage in which tritium‐hydrogen exchange and lysinoalanine formation increased. This decrease is caused by racemization of small amounts of the amino acid residue.