Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate

The hydrolysis properties of lipase in castor was evaluated using two different substrate forms (tripalmitic glycerides and trioleic glycerides) to catalyze the reaction under different operational conditions. RcLipase was obtained from castor seeds and results show that RcLipase is a conservative s...

Descripción completa

Detalles Bibliográficos
Autores principales: Li, Yue, Li, Guorui, Sun, Huajun, Chen, Yongsheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7994567/
https://www.ncbi.nlm.nih.gov/pubmed/33767251
http://dx.doi.org/10.1038/s41598-021-86305-z
_version_ 1783669778350604288
author Li, Yue
Li, Guorui
Sun, Huajun
Chen, Yongsheng
author_facet Li, Yue
Li, Guorui
Sun, Huajun
Chen, Yongsheng
author_sort Li, Yue
collection PubMed
description The hydrolysis properties of lipase in castor was evaluated using two different substrate forms (tripalmitic glycerides and trioleic glycerides) to catalyze the reaction under different operational conditions. RcLipase was obtained from castor seeds and results show that RcLipase is a conservative serine lipase with a conserved catalytic center (SDH) and a conserved pentapeptide (GXSXG). This enzyme exhibited the greatest activity and tolerance to chloroform and toluene when it was expressed in Pichia pastoris GS115 at 40 ℃ and pH 8.0. Zn and Cu ions exerted obvious inhibitory effects on the enzyme, and displayed good hydrolytic activity for long-chain natural and synthetic lipids. HPLC analysis showed that this enzyme has 1,3 regioselectivity when glycerol tripalmitate and oleic acid are used as substrates. The fatty acid composition in the reaction product was 21.3% oleic acid and 79.1% sn-2 palmitic acid.
format Online
Article
Text
id pubmed-7994567
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-79945672021-03-29 Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate Li, Yue Li, Guorui Sun, Huajun Chen, Yongsheng Sci Rep Article The hydrolysis properties of lipase in castor was evaluated using two different substrate forms (tripalmitic glycerides and trioleic glycerides) to catalyze the reaction under different operational conditions. RcLipase was obtained from castor seeds and results show that RcLipase is a conservative serine lipase with a conserved catalytic center (SDH) and a conserved pentapeptide (GXSXG). This enzyme exhibited the greatest activity and tolerance to chloroform and toluene when it was expressed in Pichia pastoris GS115 at 40 ℃ and pH 8.0. Zn and Cu ions exerted obvious inhibitory effects on the enzyme, and displayed good hydrolytic activity for long-chain natural and synthetic lipids. HPLC analysis showed that this enzyme has 1,3 regioselectivity when glycerol tripalmitate and oleic acid are used as substrates. The fatty acid composition in the reaction product was 21.3% oleic acid and 79.1% sn-2 palmitic acid. Nature Publishing Group UK 2021-03-25 /pmc/articles/PMC7994567/ /pubmed/33767251 http://dx.doi.org/10.1038/s41598-021-86305-z Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Li, Yue
Li, Guorui
Sun, Huajun
Chen, Yongsheng
Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title_full Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title_fullStr Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title_full_unstemmed Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title_short Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate
title_sort characterization of a novel sn1,3 lipase from ricinus communis l. suitable for production of oleic acid-palmitic acid-glycerol oleate
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7994567/
https://www.ncbi.nlm.nih.gov/pubmed/33767251
http://dx.doi.org/10.1038/s41598-021-86305-z
work_keys_str_mv AT liyue characterizationofanovelsn13lipasefromricinuscommunislsuitableforproductionofoleicacidpalmiticacidglycerololeate
AT liguorui characterizationofanovelsn13lipasefromricinuscommunislsuitableforproductionofoleicacidpalmiticacidglycerololeate
AT sunhuajun characterizationofanovelsn13lipasefromricinuscommunislsuitableforproductionofoleicacidpalmiticacidglycerololeate
AT chenyongsheng characterizationofanovelsn13lipasefromricinuscommunislsuitableforproductionofoleicacidpalmiticacidglycerololeate

Ejemplares similares