Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

Abstract The cold-active pectate lyases have drawn increasing attention in food and biotechnological applications due to their ability to retain high catalytic efficiency under lower temperatures, which could be helpful for energy saving, cost reduction and flavor preservation. Herein, a new cold-to...

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Autores principales:	Ling Zheng, Zilong Guo, Shengsheng Cao, Benwei Zhu
Formato:	article
Lenguaje:	EN
Publicado:	SpringerOpen 2021
Materias:	Pectate lyase Echinicola rosea Cold-adapted Product analysis Technology T Chemical technology TP1-1185 Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/d2879218d30b49d0b52ad3dfd91a9732
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spelling	oai:doaj.org-article:d2879218d30b49d0b52ad3dfd91a97322021-12-05T12:03:58ZElucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides10.1186/s40643-021-00475-22197-4365https://doaj.org/article/d2879218d30b49d0b52ad3dfd91a97322021-12-01T00:00:00Zhttps://doi.org/10.1186/s40643-021-00475-2https://doaj.org/toc/2197-4365Abstract The cold-active pectate lyases have drawn increasing attention in food and biotechnological applications due to their ability to retain high catalytic efficiency under lower temperatures, which could be helpful for energy saving, cost reduction and flavor preservation. Herein, a new cold-tolerant pectate lyase (ErPelPL1) gene from Echinicola rosea was cloned and heterologously expressed in Escherichia coli. Interestingly, ErPelPL1 retained high catalytic activity even at a low temperature (4 °C). ErPelPL1 exhibited optimal activity at 35 ℃, pH 8.0 with 1 mM of Ca2+. It showed high specific activity towards polygalacturonic acid (34.7 U/mg) and sodium polygalacturonate (59.3 U/mg). The combined thin-layer chromatography (TLC), fast protein liquid chromatography (FPLC) and electrospray ionization mass spectrometry (ESI-MS) results indicated that ErPelPL1 endolytically degraded pectic substances into the oligosaccharides with degrees of depolymerization (Dps) of 1–6. In conclusion, this study mainly conducted biochemical characterization and product analysis of a cold-tolerant pectate lyase. Therefore, it provides a promising enzyme candidate for food and biotechnological applications. Graphical AbstractLing ZhengZilong GuoShengsheng CaoBenwei ZhuSpringerOpenarticlePectate lyaseEchinicola roseaCold-adaptedProduct analysisTechnologyTChemical technologyTP1-1185BiotechnologyTP248.13-248.65ENBioresources and Bioprocessing, Vol 8, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Pectate lyase Echinicola rosea Cold-adapted Product analysis Technology T Chemical technology TP1-1185 Biotechnology TP248.13-248.65
spellingShingle	Pectate lyase Echinicola rosea Cold-adapted Product analysis Technology T Chemical technology TP1-1185 Biotechnology TP248.13-248.65 Ling Zheng Zilong Guo Shengsheng Cao Benwei Zhu Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
description	Abstract The cold-active pectate lyases have drawn increasing attention in food and biotechnological applications due to their ability to retain high catalytic efficiency under lower temperatures, which could be helpful for energy saving, cost reduction and flavor preservation. Herein, a new cold-tolerant pectate lyase (ErPelPL1) gene from Echinicola rosea was cloned and heterologously expressed in Escherichia coli. Interestingly, ErPelPL1 retained high catalytic activity even at a low temperature (4 °C). ErPelPL1 exhibited optimal activity at 35 ℃, pH 8.0 with 1 mM of Ca2+. It showed high specific activity towards polygalacturonic acid (34.7 U/mg) and sodium polygalacturonate (59.3 U/mg). The combined thin-layer chromatography (TLC), fast protein liquid chromatography (FPLC) and electrospray ionization mass spectrometry (ESI-MS) results indicated that ErPelPL1 endolytically degraded pectic substances into the oligosaccharides with degrees of depolymerization (Dps) of 1–6. In conclusion, this study mainly conducted biochemical characterization and product analysis of a cold-tolerant pectate lyase. Therefore, it provides a promising enzyme candidate for food and biotechnological applications. Graphical Abstract
format	article
author	Ling Zheng Zilong Guo Shengsheng Cao Benwei Zhu
author_facet	Ling Zheng Zilong Guo Shengsheng Cao Benwei Zhu
author_sort	Ling Zheng
title	Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
title_short	Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
title_full	Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
title_fullStr	Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
title_full_unstemmed	Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
title_sort	elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides
publisher	SpringerOpen
publishDate	2021
url	https://doaj.org/article/d2879218d30b49d0b52ad3dfd91a9732
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Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

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