{"title":"Studies on the spore coats of Aspergillus oryzae","authors":"Koki Horikoshi, Yonosuke Ikeda","doi":"10.1016/0926-6534(65)90014-X","DOIUrl":null,"url":null,"abstract":"<div><p>The distribution of β-glucosidase (EC 3.2.1.21) in dormant and germinating conidia of <em>Aspergillus oryzae</em> has been studied. A considerable amount of the bound β-glucosidase is found in the conidia coats of dormant and germinating conidia, and the ratio of bound form to soluble form in the conidia increases as germination proceeds. The bound enzyme is not removed by detergents, EDTA, urea, salts, and β-1,3-glucanase, but sonication is fairly effective. The physical and chemical properties show that the bound enzyme is identical to the soluble enzyme.</p></div>","PeriodicalId":100163,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1965-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6534(65)90014-X","citationCount":"17","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092665346590014X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 17
Abstract
The distribution of β-glucosidase (EC 3.2.1.21) in dormant and germinating conidia of Aspergillus oryzae has been studied. A considerable amount of the bound β-glucosidase is found in the conidia coats of dormant and germinating conidia, and the ratio of bound form to soluble form in the conidia increases as germination proceeds. The bound enzyme is not removed by detergents, EDTA, urea, salts, and β-1,3-glucanase, but sonication is fairly effective. The physical and chemical properties show that the bound enzyme is identical to the soluble enzyme.