{"title":"Novel acid trehalase belonging to glycoside hydrolase family 37 from <i>Pleurotus</i> sp.: cloning, expression and characterization.","authors":"Gaku Tsutsumi, Chikako Kuroki, Kengo Kamei, Mizuho Kusuda, Masami Nakazawa, Tatsuji Sakamoto, Mariko Ishikawa, Shinji Harada, Hitoshi Kobayashi, Kenji Ouchi, Satoshi Inatomi, Minoru Sakaguchi, Takeo Iwamoto, Mitsuhiro Ueda","doi":"10.47371/mycosci.2022.09.001","DOIUrl":null,"url":null,"abstract":"<p><p>The N-terminal amino acid sequence of the <i>Pleurotus</i> sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from <i>P. ostreatus</i> PC 15 v2.0. The length of the <i>Pleurotus</i> sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an <i>N</i>-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37.</p>","PeriodicalId":18780,"journal":{"name":"Mycoscience","volume":null,"pages":null},"PeriodicalIF":1.5000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/05/2b/MYC-63-284.PMC10024966.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Mycoscience","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.47371/mycosci.2022.09.001","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"MYCOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an N-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37.
期刊介绍：
Mycoscience is the official English-language journal of the Mycological Society of Japan and is issued bimonthly. Mycoscience publishes original research articles and reviews on various topics related to fungi including yeasts and other organisms that have traditionally been studied by mycologists. The research areas covered by Mycoscience extend from such purely scientific fields as systematics, evolution, phylogeny, morphology, ecology, physiology, biochemistry, genetics, and molecular biology, to agricultural, medical, and industrial applications. New and improved applications of well-established mycological techniques and methods are also covered.
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