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   <subfield code="a">Studies on properties of the xylan-binding domain and linker sequence of xylanase XynG1-1 from Paenibacillus campinasensis G1-1</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Yihan Liu, Lin Huang, Weiguo Li, Wei Guo, Hongchen Zheng, Jianling Wang, Fuping Lu]</subfield>
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   <subfield code="a">Xylanase XynG1-1 from Paenibacillus campinasensis G1-1 consists of a catalytic domain (CD), a family 6_36 carbohydrate-binding module which is a xylan-binding domain (XBD), and a linker sequence (LS) between them. The structure of XynG1-3 from Bacillus pumilus G1-3 consists only of a CD. To investigate the functions and properties of the XBD and LS of XynG1-1, two truncated forms (XynG1-1CDL, XynG1-1CD) and three fusion derivatives (XynG1-3CDL, XynG1-3CDX and XynG1-3CDLX) were constructed and biochemically characterized. The optimum conditions for the catalytic activity of mutants of XynG1-1 and XynG1-3 were 60°C and pH7.0, and 55°C and pH8.0, respectively, the same as for the corresponding wild-type enzymes. XynGs with an XBD were stable over a broad temperature (30-80°C) and pH range (4.0-11.0), respectively, on incubation for 3h. Kinetic parameters (K m , k cat, k cat/K m ) of XynGs were determined with soluble birchwood xylan and insoluble oat spelt xylan as substrates. XynGs with the XBD showed better affinities toward, and more efficient catalysis of hydrolysis of the insoluble substrate. The XBD had positive effects on thermostability and pH stability and a crucial function in the ability of the enzyme to bind and hydrolyze insoluble substrate. The LS had little effect on the overall stability of the xylanase and no relationship with affinities for soluble and insoluble substrates or catalytic efficiency.</subfield>
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   <subfield code="a">Society for Industrial Microbiology and Biotechnology, 2015</subfield>
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   <subfield code="a">Xylanase</subfield>
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   <subfield code="a">Linker sequence</subfield>
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   <subfield code="a">Enzyme properties</subfield>
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   <subfield code="u">Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, 300457, Tianjin, China</subfield>
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   <subfield code="t">Journal of Industrial Microbiology &amp; Biotechnology</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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