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Interaction between Trypsin-Like Enzyme from Streptomyces erythraeus and Chicken Ovomucoid
Abstract
Chicken ovomucoid (CO), an effective inhibitor of bovine trypsin, has a reactive site in each of three tandem domains. When CO was subjected to inhibition assay by the method of Green and Work, the second domain (CO Domain II) inhibited bovine trypsin but not TLE-Se, a trypsin-like enzyme from Streptomyces erythraeus, and the first domain (CO Domain I) inhibited neither bovine trypsin nor TLE-Se. However, when the interaction between CO and TLE-Se was analyzed by means of a Lineweaver-Burk plot, it was found that the ovomucoid exhibited competitive inhibition of the bacterial protease at pH 8.0 (Ki = 5.2 microM). In this case, the reactive-site peptide bonds of the first and second domains were specifically hydrolyzed. The isolated CO Domain I also exhibited competitive inhibition of TLE-Se (Ki = 3.1 microM), which specifically hydrolyzed its reactive-site peptide bond.
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In the citing paper
“Even the protein is considered as a trypsin inhibitor, which is a negative property of the protein; it has the capability of controlling microorganisms. Therefore, it can be used as an antimicrobial agent for foods.”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Nagata and Yoshida, 1984
In the citing paper
“Nagata and Yoshida (1984) reported that ovomucoid can be used to control Streptomyces erythraeus.”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Nagata and Yoshida, 1984
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Abeyrathne, E. D. N. S., Lee, H. Y., & Ahn, D. U. (2013) · Poultry Science · doi:10.3382/ps.2013-03391 · Cited by 532
Kato, I., Schrode, J., Kohr, W. J., & Laskowski, M. C. (1987) · Biochemistry · doi:10.1021/bi00375a027 · Cited by 204
Characteristics of protein and amino acid in various poultry egg white ovomucoid
Nurliyani, N., Erwanto, Y., Rumiyati, R., & Sukarno, A. S. (2023) · Food Science and Technology · doi:10.1590/fst.101722 · Cited by 20
Isolation and characterization of domain I of ovoinhibitor
Galzie, Z., QASIM, M. A., & Salahuddin, A. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00234-0 · Cited by 9
Abeyrathne, E. D. N. S., & Ahn, D. U. (2015) · Wageningen Academic Publishers eBooks · doi:10.3920/978-90-8686-804-9_2 · Cited by 8
Metadata
- Authors
- NAGATA, K., & YOSHIDA, N.
- Affiliations
- Shionogi (Japan) (JP)
- ORCID
- YOSHIDA, Nobuo
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 1984-10
- Volume
- 96
- Issue
- 4
- Pages
- 1041-1049
- ISSN
- 0021-924X (ISSN-L)
- 1756-2651
- OpenAlex
- W1848574081
- Cited by
- 12
- References
- 0
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 1 · 2017: 1 · 2015: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- trypsin-like enzymes, competitive inhibition, protease inhibition, reactive sites, bovine trypsin, Lineweaver-Burk kinetics, peptide bond hydrolysis
- MeSH terms
- Amino Acids, Animals, Binding, Competitive, Chickens, Egg Proteins, Kinetics, Ovomucin, Protease Inhibitors, Streptomyces, Trypsin Inhibitors
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