Thermal inactivation parameters for alkaline proteinases from north sea cod (Gadus morhua) and bovine α-chymotrypsin

Mat Amin Amiza, Richard KO Apenten

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The heat inactivation of a mixture of alkaline proteinases from North Sea cod (Gadus morhua) viscera and bovine α-chymotrypsin were compared at 40–60°C, pH 8.0. Fish digestive proteinases were at least 10-fold less heat resistant than chymotrypsin mainly as a result of a lower apparent activation enthalpy (ΔH#) for the thermoinactivation of the former proteinases.
LanguageEnglish
Pages389
JournalJournal of the Science of Food and Agriculture
Volume66
Issue number3
DOIs
Publication statusPublished - 1994

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Gadus morhua
North Sea
Gadiformes
heat inactivation
chymotrypsin
cod (fish)
Peptide Hydrolases
proteinases
Hot Temperature
Viscera
cattle
Chymotrypsin
Fishes
animal organs
enthalpy
heat
fish
alkaline protease
alpha-chymotrypsin

Cite this

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title = "Thermal inactivation parameters for alkaline proteinases from north sea cod (Gadus morhua) and bovine α-chymotrypsin",
abstract = "The heat inactivation of a mixture of alkaline proteinases from North Sea cod (Gadus morhua) viscera and bovine α-chymotrypsin were compared at 40–60°C, pH 8.0. Fish digestive proteinases were at least 10-fold less heat resistant than chymotrypsin mainly as a result of a lower apparent activation enthalpy (ΔH#) for the thermoinactivation of the former proteinases.",
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Thermal inactivation parameters for alkaline proteinases from north sea cod (Gadus morhua) and bovine α-chymotrypsin. / Amiza, Mat Amin; Apenten, Richard KO.

In: Journal of the Science of Food and Agriculture, Vol. 66, No. 3, 1994, p. 389.

Research output: Contribution to journalArticle

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AU - Apenten, Richard KO

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AB - The heat inactivation of a mixture of alkaline proteinases from North Sea cod (Gadus morhua) viscera and bovine α-chymotrypsin were compared at 40–60°C, pH 8.0. Fish digestive proteinases were at least 10-fold less heat resistant than chymotrypsin mainly as a result of a lower apparent activation enthalpy (ΔH#) for the thermoinactivation of the former proteinases.

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