Characterization of a glucoamylase immobilized on chitin

Denise Guimarães Freire, Geraldo Lippel Sant'Anna Jr.
{"title":"Characterization of a glucoamylase immobilized on chitin","authors":"Denise Guimarães Freire,&nbsp;Geraldo Lippel Sant'Anna Jr.","doi":"10.1016/0144-4565(90)90074-T","DOIUrl":null,"url":null,"abstract":"<div><p>Glucoamylase (E.C. 3.2.1.3) covalently immobilized on chitin particles (24–60 mesh) showed an average activity of 1000 U g<sup>−1</sup>. Temperature and pH optima were 60°C and 3·6, respectively. These values were lower than the corresponding ones for the free enzyme (pH 4·4, temperature 65°C). The K<sub><em>m</em></sub> (Michaelis constant) values for soluble starch and hydrolyzed manioc starch were, respectively, 1·25 and 3·94 g litre<sup>−1</sup> (free enzyme) and 8·6 and 7·8 g litre<sup>−1</sup> (immobilized enzyme).</p></div>","PeriodicalId":100179,"journal":{"name":"Biomass","volume":"23 1","pages":"Pages 71-78"},"PeriodicalIF":0.0000,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0144-4565(90)90074-T","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomass","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/014445659090074T","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7

Abstract

Glucoamylase (E.C. 3.2.1.3) covalently immobilized on chitin particles (24–60 mesh) showed an average activity of 1000 U g−1. Temperature and pH optima were 60°C and 3·6, respectively. These values were lower than the corresponding ones for the free enzyme (pH 4·4, temperature 65°C). The Km (Michaelis constant) values for soluble starch and hydrolyzed manioc starch were, respectively, 1·25 and 3·94 g litre−1 (free enzyme) and 8·6 and 7·8 g litre−1 (immobilized enzyme).

几丁质固定化葡萄糖淀粉酶的研究
葡萄糖淀粉酶(E.C. 3.2.1.3)共价固定在甲壳素颗粒(24-60目)上,平均活性为1000 U g−1。最佳温度和pH分别为60℃和3.6℃。这些值低于游离酶(pH为4·4,温度为65℃)的相应值。可溶性淀粉和水解木薯淀粉的Km (Michaelis常数)分别为1.25和3.94 g l - 1(游离酶)和8.6和7.8 g l - 1(固定化酶)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信