The Secondary Structure Analysis and Protein Identification of Esterase Were Performed by Circular Dichroism

Xinzhi Cao, Liming Zhong, Shuyuan Li, Anqi Zhou, Kaizheng Zhang, Zeli Song

2022

Abstract

In order to improve the yield of esterase and achieve the purpose of improving liquor quality rate and aroma, the structure of esterase was studied by circular dichroism method and the protein was identified by liquid mass spectrometry (LC-MS/MS). The results showed that the content of esterification enzyme Helix (Helix) was 17.10%, anti-parallel β -folding structure was 29.70%, parallel β -folding structure was 5.40%, β -rotation structure was 18.60%, irregular coil structure was 37.80%. This indicates that esterase is a kind of protein with irregular curl. The β -folding structure of esterase accounted for 35.10%, indicating that the secondary structure of esterase had a certain rigidity, but the β -rotation and random curl structure accounted for 56.40%, indicating that the various residues in esterase peptide segment had a large degree of freedom, good flexibility, but poor stability. Protein identification results showed that RHICH Lipase peptide had the highest content, 906, coverage rate of 76.35%, total theoretical amino acids of 389 protein. The number of PSEFL DNA-Binding Response regulator peptide was 14, the coverage rate was 32.93%, and the total number of theoretical amino acids was 246. Then, the number of BURPL 50S ribosomal protein L5 peptide was 10, the coverage was 18.99%, and the total number of theoretical protein amino acids was 179; Then there was 9GAMM 30S ribosomal protein S19 peptide, the number was 7, the peptide coverage was 15.22% and the total number of theoretical amino acids was 92; Finally, the peptide of 9GAMM Succinate dehydrogenase iron-sulfur subunit was 7, the coverage rate was 16.03, and the total number of protein theoretical amino acids was 237.

Paper Citation

in Harvard Style

Cao X., Zhong L., Li S., Zhou A., Zhang K. and Song Z. (2022). The Secondary Structure Analysis and Protein Identification of Esterase Were Performed by Circular Dichroism. In Proceedings of the 1st International Conference on Food Science and Biotechnology - Volume 1: FSB; ISBN 978-989-758-638-5, SciTePress, pages 76-79. DOI: 10.5220/0012002200003625

in Bibtex Style

@conference{fsb22,
author={Xinzhi Cao and Liming Zhong and Shuyuan Li and Anqi Zhou and Kaizheng Zhang and Zeli Song},
title={The Secondary Structure Analysis and Protein Identification of Esterase Were Performed by Circular Dichroism},
booktitle={Proceedings of the 1st International Conference on Food Science and Biotechnology - Volume 1: FSB},
year={2022},
pages={76-79},
publisher={SciTePress},
organization={INSTICC},
doi={10.5220/0012002200003625},
isbn={978-989-758-638-5},
}

in EndNote Style

TY - CONF

JO - Proceedings of the 1st International Conference on Food Science and Biotechnology - Volume 1: FSB
TI - The Secondary Structure Analysis and Protein Identification of Esterase Were Performed by Circular Dichroism
SN - 978-989-758-638-5
AU - Cao X.
AU - Zhong L.
AU - Li S.
AU - Zhou A.
AU - Zhang K.
AU - Song Z.
PY - 2022
SP - 76
EP - 79
DO - 10.5220/0012002200003625
PB - SciTePress