Characterization of a tannin acyl hydrolase from Streptomyces sviceus with substrate preference for digalloyl ester bonds

Verfasser / Beitragende:
[Mingbo Wu, Qin Wang, William McKinstry, Bin Ren]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/6(2015-03-01), 2663-2672
Format:
Artikel (online)
ID: 605499136
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024 7 0 |a 10.1007/s00253-014-6085-9  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-014-6085-9 
245 0 0 |a Characterization of a tannin acyl hydrolase from Streptomyces sviceus with substrate preference for digalloyl ester bonds  |h [Elektronische Daten]  |c [Mingbo Wu, Qin Wang, William McKinstry, Bin Ren] 
520 3 |a The search for new tannases with novel enzymatic properties suitable for industrial applications has been a continuous effort since the first discovery of the enzyme more than a century ago. A tannase gene (Ss-Tan) from the Gram-positive bacterium Streptomyces sviceus was identified, chemically synthesized, and cloned into a C-terminal His-tagged vector for expression in Escherichia coli. The tannase possesses the active site motif of GXSXG that is conserved for serine hydrolases. The residues that constitute the catalytic triad and galloyl binding site in bacterial tannases are found conserved in Ss-Tan, which include Ser209, Asp452, His484 and Lys370, Glu384, Asp454, respectively. Ss-Tan was overexpressed in E. coli BL21-AI cells with high productivity. Enzymatic assay revealed that the enzyme displays tannase activities to hydrolyze both the ester bonds and depside bonds in hydrolyzable tannins. Kinetic analysis indicated that the enzyme preferentially acts on depside bonds with considerably higher substrate affinity and catalytic efficiency. The enzyme showed maximum activity around pH 8.0 and at 50°C with the highest melting temperature close to 70°C. The high depsidase activity and thermostablility of Ss-Tan may make the enzyme suitable for potential industrial applications to achieve complete digestion of hydrolyzable tannins. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a Tannase  |2 nationallicence 
690 7 |a Hydrolyzable tannin  |2 nationallicence 
690 7 |a Serine hydrolase  |2 nationallicence 
690 7 |a Streptomyces  |2 nationallicence 
690 7 |a Thermostability  |2 nationallicence 
690 7 |a Kinetics  |2 nationallicence 
700 1 |a Wu  |D Mingbo  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
700 1 |a Wang  |D Qin  |u Institute of Nanobiomedical Technology and Membrane Biology, State Key Laboratory of Biotherapy, Sichuan University, 610041, Chengdu, China  |4 aut 
700 1 |a McKinstry  |D William  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
700 1 |a Ren  |D Bin  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2663-2672  |x 0175-7598  |q 99:6<2663  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-014-6085-9  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-014-6085-9  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wu  |D Mingbo  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wang  |D Qin  |u Institute of Nanobiomedical Technology and Membrane Biology, State Key Laboratory of Biotherapy, Sichuan University, 610041, Chengdu, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a McKinstry  |D William  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ren  |D Bin  |u Materials Science and Engineering, CSIRO, 343 Royal Parade, 3052, Parkville, VIC, Australia  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2663-2672  |x 0175-7598  |q 99:6<2663  |1 2015  |2 99  |o 253