INFLUENCE OF G187W/K188F/D189Y MUTATION IN THE SUBSTRATE BINDING POCKET OF TRYPSIN ON ?-CASEIN PROCESSING
Author:
Publisher
Wiley
Subject
Cell Biology,Pharmacology,Food Science,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1745-4514.1998.tb00260.x/fullpdf
Reference32 articles.
1. Inhibition of bovine trypsin by the phosphorylated N-terminal part β(1-105) of β-casein
2. Novel Opioid Peptides Derived from Casein (β-Casomorphins). I. Isolation from Bovine Casein Peptone
3. L. BRIAND, J.M. CHOBERT, N. DECLERCK, V. TRAN, J. LEONIL, D. MOLLE, and T. HAERTLE, 1998 . Impact of the Lysine-188 and Aspartic Acid-189 inversion on activity of trypsin studied by hydrolysis of synthetic substrates and beta-casein. (submitted).
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1. Cutting Edge Proteomics: Benchmarking of Six Commercial Trypsins;Journal of Proteome Research;2013-07-02
2. Activities of anionic and cationic trypsins in the temperature range from 5 to 37 degrees C. Mutant anionic trypsins as a model of cold-adapted (psychrophilic) enzymes;Biochemistry (Moscow);2003
3. Milk protein modification to improve functional and biological properties;Advances in Food and Nutrition Research;2003
4. RECENT PROGRESS IN PROCESSING OF DAIRY PROTEINS: A REVIEW;Journal of Food Biochemistry;1999-10
5. Impact of the lysine-188 and aspartic acid-189 inversion on activity of trypsin;FEBS Letters;1999-01-08
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