Proceedings of the 2015 International Conference on Industrial Technology and Management Science

Study on Preparation Technology of Enzymatic Peptides of Corbicula Fluminea

Authors
Y.L. Yang, L. Zhao, C.Q. Bai, M.L Yuan, L.L. Chen, Z.Z. Wu
Corresponding Author
Y.L. Yang
Available Online November 2015.
DOI
10.2991/itms-15.2015.256How to use a DOI?
Keywords
Corbicula Fluminea; proteolysis; orthogonal test; polypeptide
Abstract

The preparation technology of enzymatic peptides of Corbicula Fluminea was studied in this paper. Alcalase, Papain, Neutrase and Protamex were used under their own optimum pH value and temperature, with the same other parameters. The results indicated that Alcalase had the highest degree of hydrolysis (DH). The dosage of enzyme, hydrolysis time, hydrolysis temperature was further investigated. The hydrolysis parameters defined by the orthogonal test. The results showed that the temperature was 50 , the dosage of enzyme was 2%, the pH was 8.5, the substrate protein concentration was 2%, which the DH was 26.95.

Copyright
© 2015, the Authors. Published by Atlantis Press.
Open Access
This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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Volume Title
Proceedings of the 2015 International Conference on Industrial Technology and Management Science
Series
Advances in Computer Science Research
Publication Date
November 2015
ISBN
978-94-6252-123-0
ISSN
2352-538X
DOI
10.2991/itms-15.2015.256How to use a DOI?
Copyright
© 2015, the Authors. Published by Atlantis Press.
Open Access
This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

Cite this article

TY  - CONF
AU  - Y.L. Yang
AU  - L. Zhao
AU  - C.Q. Bai
AU  - M.L Yuan
AU  - L.L. Chen
AU  - Z.Z. Wu
PY  - 2015/11
DA  - 2015/11
TI  - Study on Preparation Technology of Enzymatic Peptides of Corbicula Fluminea
BT  - Proceedings of the 2015 International Conference on Industrial Technology and Management Science
PB  - Atlantis Press
SP  - 1061
EP  - 1064
SN  - 2352-538X
UR  - https://doi.org/10.2991/itms-15.2015.256
DO  - 10.2991/itms-15.2015.256
ID  - Yang2015/11
ER  -