Identification and characterization of novel intracellular α-xylosidase in <i>Aspergillus oryzae</i>

IF 1.2 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Tomohiko Matsuzawa, Yusuke Nakamichi, Naoki Shimada
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引用次数: 0

Abstract

α-Xylosidase releases xylopyranosyl side chains from xyloglucan oligosaccharides and is vital for xyloglucan degradation. Previously, we identified and characterized two α-xylosidases, intracellular AxyA and extracellular AxyB, in Aspergillus oryzae. In this study, we identified a third α-xylosidase, termed AxyC, in A. oryzae. These three A. oryzae α-xylosidases belong to the glycoside hydrolase family 31, but there are clear differences in substrate specificity. Both AxyA and AxyB showed much higher hydrolytic activity toward isoprimeverose (α-D-xylopyranosyl-1,6-glucose) than p-nitrophenyl α-D-xylopyranoside. In contrast, the specific activity of AxyC toward the p-nitrophenyl substrate was approximately 950-fold higher than that toward isoprimeverose. Our study revealed that there are multiple α-xylosidases with different substrate specificities in A. oryzae.
米曲霉胞内新型α-木糖苷酶的鉴定与表征
α-木糖苷酶从低聚木葡聚糖中释放木吡喃基侧链,对木葡聚糖的降解至关重要。此前,我们鉴定并鉴定了米曲霉胞内AxyA和胞外AxyB两种α-木糖苷酶。在这项研究中,我们鉴定出了第三种α-木糖苷酶,命名为AxyC。这三种米霉α-木糖苷酶同属糖苷水解酶家族31,但在底物特异性上存在明显差异。AxyA和AxyB对异戊糖(α- d -木pyranoyl -1,6-葡萄糖)的水解活性明显高于对硝基苯α- d -木pyranoside。相比之下,AxyC对对硝基苯底物的比活性比异戊糖高约950倍。我们的研究表明,稻瘟病菌中存在多种具有不同底物特异性的α-木糖苷酶。
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来源期刊
Journal of applied glycoscience
Journal of applied glycoscience BIOCHEMISTRY & MOLECULAR BIOLOGY-
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9.10%
发文量
13
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