{"title":"Comparison of covalent and noncovalent immobilization of Malatya apricot pectinesterase (Prunus armeniaca L.).","authors":"Emine Karakuş, Sule Pekyardımcı","doi":"10.3109/10731199.2011.611471","DOIUrl":null,"url":null,"abstract":"<p><p>Pectinesterase isolated from Malatya apricot pulp was noncovalently and covalently immobilized onto bentonite and glutaraldehyde-containing amino group functionalized porous glass beads surface at pH 8.0 and pH 9.0, respectively. The effect of various parameters such as pH, temperature, activation energy, heat and storage stability on immobilized enzyme were investigated. The optimum temperature of covalently and noncovalently immobilized PE was 50°C. This value was 60°C for free PE. Although optimum pH of covalently-immobilized PE was 8.0, this parameter was 9.0 for free and covalently-immobilized PE. The noncovalently immobilized enzyme exhibited better thermostability than the free and covalently immobilized PE.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2012-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.611471","citationCount":"9","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Artificial cells, blood substitutes, and immobilization biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10731199.2011.611471","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2011/9/27 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 9
Abstract
Pectinesterase isolated from Malatya apricot pulp was noncovalently and covalently immobilized onto bentonite and glutaraldehyde-containing amino group functionalized porous glass beads surface at pH 8.0 and pH 9.0, respectively. The effect of various parameters such as pH, temperature, activation energy, heat and storage stability on immobilized enzyme were investigated. The optimum temperature of covalently and noncovalently immobilized PE was 50°C. This value was 60°C for free PE. Although optimum pH of covalently-immobilized PE was 8.0, this parameter was 9.0 for free and covalently-immobilized PE. The noncovalently immobilized enzyme exhibited better thermostability than the free and covalently immobilized PE.
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