{"title":"米曲霉胞内新型α-木糖苷酶的鉴定与表征","authors":"Tomohiko Matsuzawa, Yusuke Nakamichi, Naoki Shimada","doi":"10.5458/jag.jag.jag-2023_0007","DOIUrl":null,"url":null,"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.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"38 1","pages":"0"},"PeriodicalIF":1.2000,"publicationDate":"2023-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification and characterization of novel intracellular α-xylosidase in <i>Aspergillus oryzae</i>\",\"authors\":\"Tomohiko Matsuzawa, Yusuke Nakamichi, Naoki Shimada\",\"doi\":\"10.5458/jag.jag.jag-2023_0007\",\"DOIUrl\":null,\"url\":null,\"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.\",\"PeriodicalId\":14999,\"journal\":{\"name\":\"Journal of applied glycoscience\",\"volume\":\"38 1\",\"pages\":\"0\"},\"PeriodicalIF\":1.2000,\"publicationDate\":\"2023-09-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of applied glycoscience\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.5458/jag.jag.jag-2023_0007\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied glycoscience","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5458/jag.jag.jag-2023_0007","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
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。
Identification and characterization of novel intracellular α-xylosidase in <i>Aspergillus oryzae</i>
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.