Klaudia Karkeszová, V. Illeová, P. Kis, V. Mastihuba, M. Polakovič
{"title":"Apin诱导曲霉产生β-葡萄糖苷酶","authors":"Klaudia Karkeszová, V. Illeová, P. Kis, V. Mastihuba, M. Polakovič","doi":"10.2478/acs-2020-0011","DOIUrl":null,"url":null,"abstract":"Abstract β-Apiosidase is a rare glycosidase applied in winemaking for flavour enhancement. This enzyme is involved in the release of volatile terpenes by hydrolysis of their odourless glycosidic precursors. It is found as a minor component in commercial pectinase/cellulase preparations. Microbial production of β-apiosidase by two Aspergillus sp. strains was investigated. Apiin-induced production of this extracellular glycosidase was confirmed only during the cultivation of Aspergillus niger CBS 554.65 but the high productivity value reported in the work of Dupin et al. (1992) J. Agric. Food Chem. 40(10): 1886—1891 could not be reproduced. The achieved productivity was by far not satisfactory considering the apiin cost. Commercial enzyme preparations with β-apiosidase side-activity thus remain a better alternative as the enzyme source for biocatalytic applications.","PeriodicalId":7088,"journal":{"name":"Acta Chimica Slovaca","volume":null,"pages":null},"PeriodicalIF":0.9000,"publicationDate":"2020-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Apiin-induction of β-apiosidase production by Aspergillus sp. strains\",\"authors\":\"Klaudia Karkeszová, V. Illeová, P. Kis, V. Mastihuba, M. Polakovič\",\"doi\":\"10.2478/acs-2020-0011\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Abstract β-Apiosidase is a rare glycosidase applied in winemaking for flavour enhancement. This enzyme is involved in the release of volatile terpenes by hydrolysis of their odourless glycosidic precursors. It is found as a minor component in commercial pectinase/cellulase preparations. Microbial production of β-apiosidase by two Aspergillus sp. strains was investigated. Apiin-induced production of this extracellular glycosidase was confirmed only during the cultivation of Aspergillus niger CBS 554.65 but the high productivity value reported in the work of Dupin et al. (1992) J. Agric. Food Chem. 40(10): 1886—1891 could not be reproduced. The achieved productivity was by far not satisfactory considering the apiin cost. Commercial enzyme preparations with β-apiosidase side-activity thus remain a better alternative as the enzyme source for biocatalytic applications.\",\"PeriodicalId\":7088,\"journal\":{\"name\":\"Acta Chimica Slovaca\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.9000,\"publicationDate\":\"2020-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta Chimica Slovaca\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2478/acs-2020-0011\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Chimica Slovaca","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2478/acs-2020-0011","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Apiin-induction of β-apiosidase production by Aspergillus sp. strains
Abstract β-Apiosidase is a rare glycosidase applied in winemaking for flavour enhancement. This enzyme is involved in the release of volatile terpenes by hydrolysis of their odourless glycosidic precursors. It is found as a minor component in commercial pectinase/cellulase preparations. Microbial production of β-apiosidase by two Aspergillus sp. strains was investigated. Apiin-induced production of this extracellular glycosidase was confirmed only during the cultivation of Aspergillus niger CBS 554.65 but the high productivity value reported in the work of Dupin et al. (1992) J. Agric. Food Chem. 40(10): 1886—1891 could not be reproduced. The achieved productivity was by far not satisfactory considering the apiin cost. Commercial enzyme preparations with β-apiosidase side-activity thus remain a better alternative as the enzyme source for biocatalytic applications.