Campus Units

Chemical and Biological Engineering

Document Type

Article

Research Focus Area

Biorenewables

Publication Version

Published Version

Publication Date

7-1989

Journal or Book Title

Journal of Agricultural and Food Chemistry

Volume

37

Issue

4

First Page

1188

Last Page

1192

DOI

10.1021/jf00088a081

Abstract

Corn gluten meal was hydrolyzed with Alcalase 2.4L, an alkaline protease. The effects of enzyme concentration and gluten size reduction on the hydrolysis were studied. Extent of reaction was expressed in terms of both the degree of hydrolysis (using the pH-stat technique) and the concentration of soluble protein. Linear and product inhibition kinetic models were compared to the experimental results after parameter estimation by minimizing the residual sum of squares. The models describe the time-dependent behavior of three protein/peptide pools-insoluble protein, TCA-insoluble proteins, and TCA-soluble peptides. A simplified product inhibition model gave the best fit to the experimental data.

Comments

Reprinted with permission from Journal of Agricultural and Food Chemistry 37 (1989): 1188–1192, doi:10.1021/jf00088a081.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

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