Please use this identifier to cite or link to this item: https://doi.org/10.15480/882.2239
Publisher DOI: 10.3389/fbioe.2015.00076
Title: First Glycoside Hydrolase Family 2 Enzymes from Thermus antranikianii and Thermus brockianus with β-Glucosidase Activity
Language: English
Authors: Schröder, Carola 
Blank, Saskia 
Antranikian, Garabed 
Keywords: β-glucosidase;glycoside hydrolase;thermostable;thermus antranikianii;thermus brockianus;cellobiose;truncated domains
Issue Date: 3-Jun-2015
Source: Frontiers in bioengineering and biotechnology (3): 1-9 (2015)
Journal or Series Name: Frontiers in Bioengineering and Biotechnology 
Abstract (english): Two glycoside hydrolase encoding genes (tagh2 and tbgh2) were identified from different Thermus species using functional screening. Based on amino acid similarities, the enzymes were predicted to belong to glycoside hydrolase (GH) family 2. Surprisingly, both enzymes (TaGH2 and TbGH2) showed twofold higher activities for the hydrolysis of nitrophenol-linked β-D-glucopyranoside than of -galactopyranoside. Specific activities of 3,966 U/mg for TaGH2 and 660 U/mg for TbGH2 were observed. In accordance, K m values for both enzymes were significantly lower when β-D-glucopyranoside was used as substrate. Furthermore, TaGH2 was able to hydrolyze cellobiose. TaGH2 and TbGH2 exhibited highest activity at 95 and 90°C at pH 6.5. Both enzymes were extremely thermostable and showed thermal activation up to 250% relative activity at temperatures of 50 and 60°C. Especially, TaGH2 displayed high tolerance toward numerous metal ions (Cu(2+), Co(2+), Zn(2+)), which are known as glycoside hydrolase inhibitors. In this study, the first thermoactive GH family 2 enzymes with β-glucosidase activity have been identified and characterized. The hydrolysis of cellobiose is a unique property of TaGH2 when compared to other enzymes of GH family 2. Our work contributes to a broader knowledge of substrate specificities in GH family 2.
URI: http://hdl.handle.net/11420/2613
DOI: 10.15480/882.2239
ISSN: 2296-4185
Institute: Technische Mikrobiologie V-7 
Type: (wissenschaftlicher) Artikel
Funded by: German Federal Ministry of Education and Research (BMBF), German Research Foundation (DFG)
Appears in Collections:Publications (tub.dok)

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