NDLI: Gene clone and characterization of a novel thermostable β-galactosidase with transglycosylation activity from Thermotoga naphthophila RUK-10

Content Provider	Springer Nature Link
Author	Wang, Man Di, Xiangjun Gao, Renjun Yang, Jingwen
Copyright Year	2015
Abstract	We cloned and expressed a new recombinant β-galactosidase(TN0949) from Thermotoga naphthophila RKU-10 with the pET28a(+) vector system in Escherichia coli BL21(DE3), and determined its catalytic capability to synthesize alkyl glucosides. The recombinant enzyme was purified to a single band via heat treatment and Ni$^{2+}$-NTA affinity chromatography. The molecular mass of the recombinant enzyme was estimated to be 79 kDa with sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE). TN0949 can hydrolyze o-nitrophenyl β-D-galactopyranoside at the optimum pH and temperature of 6.5 and 80 °C, respectively. TN0949 can also hydrolyze lactose at the optimum pH and temperature of 5.2 and 80 °C, respectively. The K $_{m}$ values for the hydrolyses of o-nitrophenyl β-D-galactopyranoside and lactose were 0.82 and 83.65 mmol/L, respectively. TN0949 was stable over a wide range of pH(3.0 to 7.0) after 24 h of incubation. The half-lives of TN0949 at 75, 80 and 85 °C were 22, 6 and 1.33 h, respectively. The enzyme displayed the capability to use lactose as the transglycosylation substrate to synthesize butyl galactopyranoside and hexyl galactopyranoside, indicating its suitability as a candidate industrial biocatalyst.
Starting Page	564
Ending Page	568
Page Count	5
File Format	PDF
ISSN	10059040
Journal	Chemical Research in Chinese Universities
Volume Number	31
Issue Number	4
e-ISSN	22103171
Language	English
Publisher	Jilin University and The Editorial Department of Chemical Research in Chinese Universities
Publisher Date	2015-06-11
Publisher Place	Changchun
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Transglycosylation Chemistry/Food Science Analytical Chemistry Physical Chemistry Thermostable Inorganic Chemistry β-Galactosidase Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Chemistry Education

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Gene cloning and molecular characterization of a β-glucosidase from Thermotoga naphthophila RUK-10: an effective tool for synthesis of galacto-oligosaccharide and alkyl galactopyranosides

A novel thermostable β-galactosidase from Geobacillus kaustophilus HTA42

Clone, purification and characterization of thermostable aminopeptidase ST1737 from Sulfolobus tokodaii

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Characterization of a Glycoside Hydrolase Family 1 β-Galactosidase from Hot Spring Metagenome with Transglycosylation Activity

Galacto-oligosaccharide production by a thermostable recombinant β-galactosidase from Thermotoga maritima

Synthesis, micellization and characterization of novel amphiphilic β-cyclodextrin/poly(L-aspartate) copolymer

Purification and characterization of two thermostable glucoamylases produced from Aspergillus niger B-30

Cloning, purification, and characterization of xylose isomerase from Thermotoga naphthophila RKU-10

Gene clone and characterization of a novel thermostable β-galactosidase with transglycosylation activity from Thermotoga naphthophila RUK-10

Similar Documents

Gene cloning and molecular characterization of a β-glucosidase from Thermotoga naphthophila RUK-10: an effective tool for synthesis of galacto-oligosaccharide and alkyl galactopyranosides

A novel thermostable β-galactosidase from Geobacillus kaustophilus HTA42

Clone, purification and characterization of thermostable aminopeptidase ST1737 from Sulfolobus tokodaii

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Characterization of a Glycoside Hydrolase Family 1 β-Galactosidase from Hot Spring Metagenome with Transglycosylation Activity

Galacto-oligosaccharide production by a thermostable recombinant β-galactosidase from Thermotoga maritima

Synthesis, micellization and characterization of novel amphiphilic β-cyclodextrin/poly(L-aspartate) copolymer

Purification and characterization of two thermostable glucoamylases produced from Aspergillus niger B-30

Cloning, purification, and characterization of xylose isomerase from Thermotoga naphthophila RKU-10

Gene clone and characterization of a novel thermostable β-galactosidase with transglycosylation activity from Thermotoga naphthophila RUK-10