Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae

Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subu...
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Autor*in:	Lin Ge [verfasserIn] Jingcong Xie Tao Wu Shanshan Zhang Linguo Zhao Gang Ding Zhenzhong Wang Wei Xiao

Format:	Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose

Übergeordnetes Werk:	Enthalten in: International journal of food science & technology - Oxford : Blackwell, 1987, 52(2017), 12, Seite 2596
Übergeordnetes Werk:	volume:52 ; year:2017 ; number:12 ; pages:2596

Links:	Volltext Link aufrufen

DOI / URN:	10.1111/ijfs.13546

Katalog-ID:	OLC1998901092

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245	1	0	\|a Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae
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520			\|a Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry.
650		4	\|a Ultrafiltration
650		4	\|a Gel filtration
650		4	\|a Food industry
650		4	\|a Mannitol
650		4	\|a Food processing industry
650		4	\|a Substrates
650		4	\|a Enzymes
650		4	\|a Thermal stability
650		4	\|a Purification
650		4	\|a pH effects
650		4	\|a L-Rhamnosidase
650		4	\|a Rhamnose
700	0		\|a Jingcong Xie \|4 oth
700	0		\|a Tao Wu \|4 oth
700	0		\|a Shanshan Zhang \|4 oth
700	0		\|a Linguo Zhao \|4 oth
700	0		\|a Gang Ding \|4 oth
700	0		\|a Zhenzhong Wang \|4 oth
700	0		\|a Wei Xiao \|4 oth
773	0	8	\|i Enthalten in \|t International journal of food science & technology \|d Oxford : Blackwell, 1987 \|g 52(2017), 12, Seite 2596 \|w (DE-627)130679712 \|w (DE-600)883561-5 \|w (DE-576)016221885 \|x 0950-5423 \|7 nnns
773	1	8	\|g volume:52 \|g year:2017 \|g number:12 \|g pages:2596
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allfields	10.1111/ijfs.13546 doi PQ20171228 (DE-627)OLC1998901092 (DE-599)GBVOLC1998901092 (PRQ)p579-a06c418cfae7ab1eb4935dbb0fe77cb5b2a9b8f1befb10e8da94358aee20dc0a0 (KEY)0040074220170000052001202596purificationandcharacterisationofanovelalphalrhamn DE-627 ger DE-627 rakwb eng 630 640 610 660 DE-600 Lin Ge verfasserin aut Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry. Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose Jingcong Xie oth Tao Wu oth Shanshan Zhang oth Linguo Zhao oth Gang Ding oth Zhenzhong Wang oth Wei Xiao oth Enthalten in International journal of food science & technology Oxford : Blackwell, 1987 52(2017), 12, Seite 2596 (DE-627)130679712 (DE-600)883561-5 (DE-576)016221885 0950-5423 nnns volume:52 year:2017 number:12 pages:2596 http://dx.doi.org/10.1111/ijfs.13546 Volltext https://search.proquest.com/docview/1962132999 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 52 2017 12 2596
spelling	10.1111/ijfs.13546 doi PQ20171228 (DE-627)OLC1998901092 (DE-599)GBVOLC1998901092 (PRQ)p579-a06c418cfae7ab1eb4935dbb0fe77cb5b2a9b8f1befb10e8da94358aee20dc0a0 (KEY)0040074220170000052001202596purificationandcharacterisationofanovelalphalrhamn DE-627 ger DE-627 rakwb eng 630 640 610 660 DE-600 Lin Ge verfasserin aut Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry. Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose Jingcong Xie oth Tao Wu oth Shanshan Zhang oth Linguo Zhao oth Gang Ding oth Zhenzhong Wang oth Wei Xiao oth Enthalten in International journal of food science & technology Oxford : Blackwell, 1987 52(2017), 12, Seite 2596 (DE-627)130679712 (DE-600)883561-5 (DE-576)016221885 0950-5423 nnns volume:52 year:2017 number:12 pages:2596 http://dx.doi.org/10.1111/ijfs.13546 Volltext https://search.proquest.com/docview/1962132999 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 52 2017 12 2596
allfields_unstemmed	10.1111/ijfs.13546 doi PQ20171228 (DE-627)OLC1998901092 (DE-599)GBVOLC1998901092 (PRQ)p579-a06c418cfae7ab1eb4935dbb0fe77cb5b2a9b8f1befb10e8da94358aee20dc0a0 (KEY)0040074220170000052001202596purificationandcharacterisationofanovelalphalrhamn DE-627 ger DE-627 rakwb eng 630 640 610 660 DE-600 Lin Ge verfasserin aut Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry. Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose Jingcong Xie oth Tao Wu oth Shanshan Zhang oth Linguo Zhao oth Gang Ding oth Zhenzhong Wang oth Wei Xiao oth Enthalten in International journal of food science & technology Oxford : Blackwell, 1987 52(2017), 12, Seite 2596 (DE-627)130679712 (DE-600)883561-5 (DE-576)016221885 0950-5423 nnns volume:52 year:2017 number:12 pages:2596 http://dx.doi.org/10.1111/ijfs.13546 Volltext https://search.proquest.com/docview/1962132999 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 52 2017 12 2596
allfieldsGer	10.1111/ijfs.13546 doi PQ20171228 (DE-627)OLC1998901092 (DE-599)GBVOLC1998901092 (PRQ)p579-a06c418cfae7ab1eb4935dbb0fe77cb5b2a9b8f1befb10e8da94358aee20dc0a0 (KEY)0040074220170000052001202596purificationandcharacterisationofanovelalphalrhamn DE-627 ger DE-627 rakwb eng 630 640 610 660 DE-600 Lin Ge verfasserin aut Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry. Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose Jingcong Xie oth Tao Wu oth Shanshan Zhang oth Linguo Zhao oth Gang Ding oth Zhenzhong Wang oth Wei Xiao oth Enthalten in International journal of food science & technology Oxford : Blackwell, 1987 52(2017), 12, Seite 2596 (DE-627)130679712 (DE-600)883561-5 (DE-576)016221885 0950-5423 nnns volume:52 year:2017 number:12 pages:2596 http://dx.doi.org/10.1111/ijfs.13546 Volltext https://search.proquest.com/docview/1962132999 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 52 2017 12 2596
allfieldsSound	10.1111/ijfs.13546 doi PQ20171228 (DE-627)OLC1998901092 (DE-599)GBVOLC1998901092 (PRQ)p579-a06c418cfae7ab1eb4935dbb0fe77cb5b2a9b8f1befb10e8da94358aee20dc0a0 (KEY)0040074220170000052001202596purificationandcharacterisationofanovelalphalrhamn DE-627 ger DE-627 rakwb eng 630 640 610 660 DE-600 Lin Ge verfasserin aut Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry. Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose Jingcong Xie oth Tao Wu oth Shanshan Zhang oth Linguo Zhao oth Gang Ding oth Zhenzhong Wang oth Wei Xiao oth Enthalten in International journal of food science & technology Oxford : Blackwell, 1987 52(2017), 12, Seite 2596 (DE-627)130679712 (DE-600)883561-5 (DE-576)016221885 0950-5423 nnns volume:52 year:2017 number:12 pages:2596 http://dx.doi.org/10.1111/ijfs.13546 Volltext https://search.proquest.com/docview/1962132999 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 52 2017 12 2596
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topic_facet	Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose
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topic_title	630 640 610 660 DE-600 Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae Ultrafiltration Gel filtration Food industry Mannitol Food processing industry Substrates Enzymes Thermal stability Purification pH effects L-Rhamnosidase Rhamnose
topic	ddc 630 misc Ultrafiltration misc Gel filtration misc Food industry misc Mannitol misc Food processing industry misc Substrates misc Enzymes misc Thermal stability misc Purification misc pH effects misc L-Rhamnosidase misc Rhamnose
topic_unstemmed	ddc 630 misc Ultrafiltration misc Gel filtration misc Food industry misc Mannitol misc Food processing industry misc Substrates misc Enzymes misc Thermal stability misc Purification misc pH effects misc L-Rhamnosidase misc Rhamnose
topic_browse	ddc 630 misc Ultrafiltration misc Gel filtration misc Food industry misc Mannitol misc Food processing industry misc Substrates misc Enzymes misc Thermal stability misc Purification misc pH effects misc L-Rhamnosidase misc Rhamnose
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hierarchy_parent_title	International journal of food science & technology
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dewey-tens	630 - Agriculture 640 - Home & family management 610 - Medicine & health 660 - Chemical engineering
hierarchy_top_title	International journal of food science & technology
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title	Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae
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title_full	Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae
author_sort	Lin Ge
journal	International journal of food science & technology
journalStr	International journal of food science & technology
lang_code	eng
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container_start_page	2596
author_browse	Lin Ge
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class	630 640 610 660 DE-600
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author-letter	Lin Ge
doi_str_mv	10.1111/ijfs.13546
dewey-full	630 640 610 660
title_sort	purification and characterisation of a novel [alpha]-l-rhamnosidase exhibiting transglycosylating activity from aspergillus oryzae
title_auth	Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae
abstract	Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry.
abstractGer	Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry.
abstract_unstemmed	Summary A novel [alpha]-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5-7.0, and it showed good thermostability at higher temperatures. The KM, kcat and kcat/KM values were 5.2 mm, 1624 s-1 and 312 s-1 mm-1 using pNPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry.
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container_issue	12
title_short	Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae
url	http://dx.doi.org/10.1111/ijfs.13546 https://search.proquest.com/docview/1962132999
remote_bool	false
author2	Jingcong Xie Tao Wu Shanshan Zhang Linguo Zhao Gang Ding Zhenzhong Wang Wei Xiao
author2Str	Jingcong Xie Tao Wu Shanshan Zhang Linguo Zhao Gang Ding Zhenzhong Wang Wei Xiao
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doi_str	10.1111/ijfs.13546
up_date	2024-07-04T05:57:29.257Z
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Purification and characterisation of a novel [alpha]-L-rhamnosidase exhibiting transglycosylating activity from Aspergillus oryzae

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