多功能糖苷水解酶：来自婴儿双歧杆菌亚种ATCC 15697的Blon_0625。
Multi-functional glycoside hydrolase: Blon_0625 from Bifidobacterium longum subsp. infantis ATCC 15697.
作者信息
Matsumoto Takuya, Shimada Shota, Hata Yuto, Tanaka Tsutomu, Kondo Akihiko
机构信息
Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodaicho, Nada, Kobe 657-8501, Japan.
Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodaicho, Nada, Kobe 657-8501, Japan.
出版信息
Enzyme Microb Technol. 2015 Jan;68:10-4. doi: 10.1016/j.enzmictec.2014.10.001. Epub 2014 Oct 22.
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 recombinant Blon_0625 retains hydrolyzing activity against both p-nitrophenyl-β-D-glucopyranoside (pNPG; 17.3±0.24Umg(-1)) and p-nitrophenyl-β-D-xylopyranoside (pNPX; 16.7±0.32Umg(-1)) at pH 6.0, 30°C. To best of our knowledge, no previously described BGL retains the same level of both pNPGase and pNPXase activity. Furthermore, Blon_0625 also retains the activity against 4-nitrophenyl-α-l-arabinofranoside (pNPAf; 5.6±0.09Umg(-1)). In addition, the results of the degradation of phosphoric acid swollen cellulose (PASC) or xylan using endoglucanase from Thermobifida fusca YX (Tfu_0901) or xylanase from Kitasatospora setae KM-6054 (KSE_59480) show that Blon_0625 acts as a BGL and as a β-D-xylosidase (XYL) for hydrolyzing oligosaccharides. These results clearly indicate that Blon_0625 is a multi-functional glycoside hydrolase which retains the activity of BGL, XYL, and also α-l-arabinofuranosidase. Therefore, the utilization of multi-functional Blon_0625 may contribute to facilitating the efficient degradation of lignocellulosic materials and help enhance bioconversion processes.
我们在此描述了一种源自婴儿双歧杆菌亚种ATCC 15697的独特β-D-葡萄糖苷酶（BGL；Blon_0625）。Blon_0625基因由重组大肠杆菌表达。纯化后的重组Blon_0625在pH 6.0、30°C条件下，对对硝基苯基-β-D-吡喃葡萄糖苷（pNPG；17.3±0.24Umg(-1)）和对硝基苯基-β-D-吡喃木糖苷（pNPX；16.7±0.32Umg(-1)）均保留水解活性。据我们所知，此前描述的BGL均未同时保留相同水平的pNPGase和pNPXase活性。此外，Blon_0625对4-硝基苯基-α-L-阿拉伯呋喃糖苷（pNPAf；5.6±0.09Umg(-1)）也保留活性。另外，使用嗜热栖热放线菌YX的内切葡聚糖酶（Tfu_0901）或北里链霉菌KM-6054的木聚糖酶（KSE_59480）对磷酸膨胀纤维素（PASC）或木聚糖进行降解的结果表明，Blon_0625可作为BGL和β-D-木糖苷酶（XYL）来水解寡糖。这些结果清楚地表明，Blon_0625是一种多功能糖苷水解酶，保留了BGL、XYL以及α-L-阿拉伯呋喃糖苷酶的活性。因此，多功能Blon_0625的应用可能有助于促进木质纤维素材料的有效降解，并有助于增强生物转化过程。
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