MULTIVARIATE ANALYSIS OF STRUCTURE-RELATED DATA TO EXPLAIN MILK CLOTTING ACTIVITY OF PROTEOLYTIC ENZYMES
- 1 June 1987
- journal article
- research article
- Published by Hindawi Limited in Journal of Food Biochemistry
- Vol. 11 (2) , 121-132
- https://doi.org/10.1111/j.1745-4514.1987.tb00117.x
Abstract
Multivariate analysis was used for investigating the relationships between milk-clotting activity and physical/chemical properties, such as CD spectra, hydrophobicity and zeta potential, of ten proteolytic enzymes measured at six different pH values. Cluster analysis of CD data and zeta potential values classified the enzymes into five groups, i.e., three active enzyme groups and two inactive enzyme groups with respect to milk clotting activity. Classification of the enzymes into three groups, i.e., enzymes with high, medium and low milk-clotting activity, was achieved by discriminant analysis after adding the ratio of secondary structure parameters to the predictor variables. Results indicated that β-sheet, β-turn and random structure features were important for milk-clotting activity.This publication has 5 references indexed in Scilit:
- Use of principal component analysis to study the relationship between physical/chemical properties and the milk-clotting to proteolysis activity ratio of some aspartyl proteinasesJournal of Agricultural and Food Chemistry, 1986
- Quantitative structure-activity relationships employing independent quantum chemical indexesJournal of Medicinal Chemistry, 1983
- UPublished by Springer Nature ,1983
- Estimation of globular protein secondary structure from circular dichroismBiochemistry, 1981
- Circular dichroic analysis of protein conformation: Inclusion of the β-turnsAnalytical Biochemistry, 1978