Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)

Abstract BACKGROUND The ability of Antarctic krill, Euphausia superba (Dana, 1852), to thrive in a cold environment comes from its capacity to synthesize cold‐adapted enzymes. Its trypsin, as a main substance in the metabolic reactions, plays a key role in the adaption to low temperatures. However,...

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Published in:Journal of the Science of Food and Agriculture
Main Authors: Zhou, Tingting, Wang, Xichang, Yan, Juan, Li, Yan
Other Authors: Shanghai Jiao Tong University
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2018
Subjects:
Online Access:http://dx.doi.org/10.1002/jsfa.8804
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spelling crwiley:10.1002/jsfa.8804 2024-09-09T19:10:14+00:00 Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852) Zhou, Tingting Wang, Xichang Yan, Juan Li, Yan Shanghai Jiao Tong University 2018 http://dx.doi.org/10.1002/jsfa.8804 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsfa.8804 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.8804 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of the Science of Food and Agriculture volume 98, issue 8, page 3049-3056 ISSN 0022-5142 1097-0010 journal-article 2018 crwiley https://doi.org/10.1002/jsfa.8804 2024-08-09T04:28:56Z Abstract BACKGROUND The ability of Antarctic krill, Euphausia superba (Dana, 1852), to thrive in a cold environment comes from its capacity to synthesize cold‐adapted enzymes. Its trypsin, as a main substance in the metabolic reactions, plays a key role in the adaption to low temperatures. However, the progress of research on its cold‐adaption mechanism is being influenced due to the limited information on its gene and spatial structure. RESULTS We studied the gene of E. superba trypsin with transcriptome sequencing first, and then discussed its cold‐adaption mechanism with the full gene and predicted structure basing on bioinformatics. The results showed the proportion of certain residues played important roles in the cold‐adaptation behavior for trypsin. Furthermore, a higher proportion of random coils and reduced steric hindrance might also be key factors promoting its cold adaption. CONCLUSION This research aimed to reveal the cold‐adaption mechanism of E. superba trypsin and provide support for basic research on molecular modification by site‐directed mutagenesis of complementary DNA used to produce new and improved recombinant variants with cold adaption. Furthermore, it may broaden its commercial application on minimizing undesirable changes elevated at higher temperature in food processing and in treatment of trauma and inflammation in medicine. © 2017 Society of Chemical Industry Article in Journal/Newspaper Antarc* Antarctic Antarctic Krill Euphausia superba Wiley Online Library Antarctic Journal of the Science of Food and Agriculture
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract BACKGROUND The ability of Antarctic krill, Euphausia superba (Dana, 1852), to thrive in a cold environment comes from its capacity to synthesize cold‐adapted enzymes. Its trypsin, as a main substance in the metabolic reactions, plays a key role in the adaption to low temperatures. However, the progress of research on its cold‐adaption mechanism is being influenced due to the limited information on its gene and spatial structure. RESULTS We studied the gene of E. superba trypsin with transcriptome sequencing first, and then discussed its cold‐adaption mechanism with the full gene and predicted structure basing on bioinformatics. The results showed the proportion of certain residues played important roles in the cold‐adaptation behavior for trypsin. Furthermore, a higher proportion of random coils and reduced steric hindrance might also be key factors promoting its cold adaption. CONCLUSION This research aimed to reveal the cold‐adaption mechanism of E. superba trypsin and provide support for basic research on molecular modification by site‐directed mutagenesis of complementary DNA used to produce new and improved recombinant variants with cold adaption. Furthermore, it may broaden its commercial application on minimizing undesirable changes elevated at higher temperature in food processing and in treatment of trauma and inflammation in medicine. © 2017 Society of Chemical Industry
author2 Shanghai Jiao Tong University
format Article in Journal/Newspaper
author Zhou, Tingting
Wang, Xichang
Yan, Juan
Li, Yan
spellingShingle Zhou, Tingting
Wang, Xichang
Yan, Juan
Li, Yan
Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
author_facet Zhou, Tingting
Wang, Xichang
Yan, Juan
Li, Yan
author_sort Zhou, Tingting
title Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
title_short Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
title_full Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
title_fullStr Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
title_full_unstemmed Gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill Euphausia superba (Dana, 1852)
title_sort gene analysis and structure prediction for the cold‐adaption mechanism of trypsin from the krill euphausia superba (dana, 1852)
publisher Wiley
publishDate 2018
url http://dx.doi.org/10.1002/jsfa.8804
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsfa.8804
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.8804
geographic Antarctic
geographic_facet Antarctic
genre Antarc*
Antarctic
Antarctic Krill
Euphausia superba
genre_facet Antarc*
Antarctic
Antarctic Krill
Euphausia superba
op_source Journal of the Science of Food and Agriculture
volume 98, issue 8, page 3049-3056
ISSN 0022-5142 1097-0010
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/jsfa.8804
container_title Journal of the Science of Food and Agriculture
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