Kinetics of Thermal Inactivation of Chicken Pepsin

Thermal inactivation of chicken pepsin was studied at pH 3, 4, and 6. Application of heat to enzyme solutions in capillary tubes enabled attainment of short come-up times. Enzyme denaturation followed first order reaction kinetics, exhibiting reasonably high thermal resistance. Activation energies o...

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Bibliographic Details
Published inJournal of dairy science Vol. 66; no. 5; pp. 981 - 983
Main Authors Kopelman, I.J., Cogan, U.
Format Journal Article
LanguageEnglish
Published Champaign Elsevier Inc 01.05.1983
Am Dairy Sci Assoc
American Dairy Science Association
Subjects
chickens
heat inactivation
pepsin
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Summary:Thermal inactivation of chicken pepsin was studied at pH 3, 4, and 6. Application of heat to enzyme solutions in capillary tubes enabled attainment of short come-up times. Enzyme denaturation followed first order reaction kinetics, exhibiting reasonably high thermal resistance. Activation energies of denaturation were 25.6, 28.0, and 30.0 kcal/mole for pH 6, 4, and 3, respectively. These are considerably lower than corresponding activation energies for other commonly utilized milk clotting enzymes. Thermal resistance and low activation energy of denaturation of chicken pepsin calls for care to inactivate properly the residual enzyme of whey products where its proteolytic activity may be undesirable.
Bibliography:8274831
Q20
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(83)81890-6