Multi-functional glycoside hydrolase: Blon_0625 from Bifidobacterium longum subsp. infantis ATCC 15697
作者： Takuya Matsumoto , Shota Shimada , Yuto Hata , Tsutomu Tanaka , Akihiko Kondo
DOI: 10.1016/J.ENZMICTEC.2014.10.001
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摘要: Abstract We here describe a unique β-D-glucosidase (BGL; Blon_0625) derived from Bifidobacterium longum subsp. infantis ATCC 15697. The Blon_0625 gene was expressed by recombinant Escherichia coli. Purified retains hydrolyzing activity against both p-nitrophenyl-β-D-glucopyranoside (pNPG; 17.3 ± 0.24 U mg−1) and p-nitrophenyl-β-D-xylopyranoside (pNPX; 16.7 ± 0.32 U mg−1) at pH 6.0, 30 °C. To best of our knowledge, no previously described BGL the same level pNPGase pNPXase activity. Furthermore, also 4-nitrophenyl-α- l -arabinofranoside (pNPAf; 5.6 ± 0.09 U mg−1). In addition, results degradation phosphoric acid swollen cellulose (PASC) or xylan using endoglucanase Thermobifida fusca YX (Tfu_0901) xylanase Kitasatospora setae KM-6054 (KSE_59480) show that acts as β-D-xylosidase (XYL) for oligosaccharides. These clearly indicate is multi-functional glycoside hydrolase which BGL, XYL, α- -arabinofuranosidase. Therefore, utilization may contribute to facilitating efficient lignocellulosic materials help enhance bioconversion processes.
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