Purification and characterization of three alkaline endopolygalacturonases from a newly isolated Bacillus gibsonii

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dc.contributor.authorLi, Z.
dc.contributor.authorJin, B.
dc.contributor.authorZhang, H.
dc.contributor.authorBai, Z.
dc.contributor.authorXue, W.
dc.contributor.authorLi, H.
dc.date.issued2008
dc.description.abstractA newly isolated Bacillus gibsonii, designated as S-2 (CGMCC1215), was cultivated for production of alkaline pectinases utilizing sugar beet pulp as growth substrate. Purification of three alkaline endopolygalacturonases (endoPGs) from the crude pectinases extract was carried out by ultra-filtration, ammonium sulphate fractionation and ion-exchange chromatography, and their enzyme activities characterized. The three purified alkaline endoPGs, designated as S-I, S-II, and S-III, had a molecular weight about 38 kDa as determined by SDS-PAGE. The K<inf>m</inf> value and optimal temperature for optimal enzyme activities of S-I, S-II and S-III were 1.2 mg/mL and 60°C, 0.9 mg/mL and 55°C, 1.1 mg/mL and 60°C, respectively. Their best performances were given at an optimal pH 10.5, and sodium polygalacturonate was found to be the best substrate. The isoelectric points of S-I, S-II and S-III were 5.4, 7.4, and 8.2, respectively. Surfactants of Tween-80 and Tween-20 and metal ions such as Mg<sup>2+</sup> and Ca<sup>2+</sup> stimulated the activity of S-I, S-II and S-III, whereas S-III was inhibited by Ca<sup>2+</sup>, and Mn<sup>2+</sup> and Zn<sup>2+</sup> ions inhibited the activity of the three enzymes.
dc.description.statementofresponsibilityLI, Zu-ming; JIN, Bo; ZHANG, Hong-xun; BAI, Zhi-hui; XUE, Wen-tong and LI, Hong-yu
dc.identifier.citationGuocheng Gongcheng Xuebao, 2008; 8(4):768-773
dc.identifier.issn1009-606X
dc.identifier.urihttp://hdl.handle.net/2440/54211
dc.language.isoen
dc.publisherKexue Chubanshe
dc.subjectalkaline endopolygalacturonases
dc.subjectBacillus gibsonii
dc.subjectpurification
dc.subjectenzyme activity
dc.titlePurification and characterization of three alkaline endopolygalacturonases from a newly isolated Bacillus gibsonii
dc.typeJournal article
pubs.publication-statusPublished

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