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THERMAL INACTIVATION KINETICS of TRYPSIN AT ASEPTIC PROCESSING TEMPERATURES
Author(s) -
AWUAH G.B.,
RAMASWAMY H.S.,
SIMPSON B.K.,
SMITH J.P.
Publication year - 1993
Publication title -
journal of food process engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 45
eISSN - 1745-4530
pISSN - 0145-8876
DOI - 10.1111/j.1745-4530.1993.tb00324.x
Subject(s) - trypsin , chemistry , kinetics , aseptic processing , chromatography , enzyme , biochemistry , nuclear chemistry , food science , physics , quantum mechanics
Kinetics of thermal inactivation of trypsin (bovine pancreas) were evaluated in the temperature range, 90–130C, common to aseptic processing of high/low acid foods. Aliquots of trypsin in buffer, at three pH values, 3.8, 5.1 and 6.0, were subjected to selected heat treatments at various temperatures. Kinetic parameters were evaluated from the residual enzyme activity. Reference k and D values (at 121.1C) ranged from 0.0719 to 0.349 min −1 and 32.0 to 6.6 min, and E a and z values ranged from 84.9 to 69.9 kJ/mole and 33.1 to 39.9C, respectively, in the pH range 3.8–6.0. the thermal inactivation resistance of trypsin in the acid and low acid pH range makes it a potential bioindicator for high temperature thermal processes.