Comparative Binding Affinity Analysis of Soybean Meal Bowman-Birk and Kunitz Trypsin Inhibitors in Interactions with Animal Serine Proteases-Reference-Cited by-同舟云学术

Comparative Binding Affinity Analysis of Soybean Meal Bowman-Birk and Kunitz Trypsin Inhibitors in Interactions with Animal Serine Proteases

Published:2023-08-08 Issue:8 Volume:3 Page:1344-1352
ISSN:2692-1944
Container-title:ACS Food Science & Technology
language:en
Short-container-title:ACS Food Sci. Technol.

Author:

Okedigba Ayoyinka O.¹²^ORCID,Rosso M. Luciana³,Yu Daisy⁴,Shang Chao³,Huang Haibo⁴^ORCID,Zhang Bo³,Capelluto Daniel G. S.¹²^ORCID

Affiliation:

1. Protein Signaling Domains Laboratory, Department of Biological Sciences, Fralin Life Sciences Institute, and Center for Soft Matter and Biological Physics, Virginia Tech, Blacksburg, Virginia 24061, United States

2. Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061, United States

3. School of Plant and Environmental Sciences, Virginia Tech, Blacksburg, Virginia 24061, United States

4. Department of Food Science and Technology, Virginia Tech, Blacksburg, Virginia 24061, United States

Funder

Virginia Polytechnic Institute and State University

United Soybean Board

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Chemistry (miscellaneous),Food Science,Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acsfoodscitech.3c00158

Reference45 articles.

1. Physiologically Active Molecules and Functional Properties of Soybeans in Human Health—A Current Perspective

2. Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

3. Nutritional and Health Benefits of Soy Proteins

4. Genetic characterization of a novel Tib-derived variant of soybean Kunitz trypsin inhibitor detected in wild soybean (Glycine soja)

5. Lectins and Protease Inhibitors as Plant Defenses against Insects

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