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Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN
An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa...
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Published in: | World journal of microbiology & biotechnology 1994-05, Vol.10 (3), p.256-259 |
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description | An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its K m value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 mM caused about 90% inhibition. |
doi_str_mv | 10.1007/BF00414857 |
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Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 mM caused about 90% inhibition.</description><identifier>ISSN: 0959-3993</identifier><identifier>EISSN: 1573-0972</identifier><identifier>DOI: 10.1007/BF00414857</identifier><identifier>PMID: 24421005</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Biological and medical sciences ; Biotechnology ; Eleusine coracana subsp. coracana ; enzyme activity ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; Improved methods for extraction and purification of enzymes ; Methods. Procedures. 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Psychology</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>Methods. Procedures. 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Technologies</topic><topic>physicochemical properties</topic><topic>polygalacturonase</topic><topic>purification</topic><topic>Rhizopus</topic><topic>starter cultures</topic><topic>tempeh</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Elegado, F.B</creatorcontrib><creatorcontrib>Fujio, Y</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>World journal of microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Elegado, F.B</au><au>Fujio, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN</atitle><jtitle>World journal of microbiology & biotechnology</jtitle><addtitle>World J Microbiol Biotechnol</addtitle><date>1994-05-01</date><risdate>1994</risdate><volume>10</volume><issue>3</issue><spage>256</spage><epage>259</epage><pages>256-259</pages><issn>0959-3993</issn><eissn>1573-0972</eissn><abstract>An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its K m value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. 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subjects | Biological and medical sciences Biotechnology Eleusine coracana subsp. coracana enzyme activity Enzyme engineering Fundamental and applied biological sciences. Psychology Improved methods for extraction and purification of enzymes Methods. Procedures. Technologies physicochemical properties polygalacturonase purification Rhizopus starter cultures tempeh |
title | Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN |
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