Full metadata record
DC FieldValueLanguage
dc.contributor.authorBai, Hongzhi-
dc.contributor.authorWang, Hui-
dc.contributor.authorSun, Junde-
dc.contributor.authorIrfan, Muhammad-
dc.contributor.authorHan, Mei-
dc.contributor.authorHuang, Yuqian-
dc.contributor.authorHan, Xiaori-
dc.contributor.authorYang, Qian-
dc.date.accessioned2014-03-10T10:33:48Z-
dc.date.available2014-03-10T10:33:48Z-
dc.date.issued2013-06-13-
dc.identifier.issn1611-2156-
dc.identifier.urihttp://hdl.handle.net/2003/32936-
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-7346-
dc.description.abstractβ-Glucosidase is an important component of the cellulase complex. It not only hydrolyzes cellobiose and short-chain cellooligos accharides to glucose, but also removes the inhibitory effect of cellobiose on the β-1, 4-endoglucanase and exoglucanase, thereby increasing the overall rate of cellulose biodegradation. β-glucosidasefrom culture supernatant of a fungus Penicillium simplicissimum was purified to homogeneity, by using ammonium sulfate fraction, Sephadex G-100 chromatography, and its properties were studied. The molecular mass of the enzyme was about 126.0 kDa, as identified by 12% SDS-PAGE. The optimum pH and temperature were 4.4 ~ 5.2 and 60°C, respectively. The enzyme was stable in pH 5.2 ~ 6.4 and under 40°C. Metal profile of the enzyme showed that Mn2+ enhances its activity, while Cu2+, Co2+ and Fe3+ cause obvious inhibition. The Km and Vmax was 14.881 mg/ml and 0.364 mg ml/min against salicin as a Substrate. This enzyme had secondary protein structure as evidenced by FTIR spectrum.en
dc.language.isoen-
dc.relation.ispartofseriesEXCLI Journal ; Vol. 12, 2013en
dc.subjectβ -Glucosidaseen
dc.subjectPenicillium simplicissimumen
dc.subjectpurificationen
dc.subjectcharacterizationen
dc.subject.ddc610-
dc.titleProduction, purification and characterization of novel beta glucosidase from newly isolated Penicillium simplicissimum H-11 in submerged fermentationen
dc.typeText-
dc.type.publicationtypearticle-
dcterms.accessRightsopen access-
eldorado.dnb.zdberstkatid2132560-1-
Appears in Collections:Original Articles

Files in This Item:
File Description SizeFormat 
Bai_13062013_proof.pdfDNB344.76 kBAdobe PDFView/Open


This item is protected by original copyright



This item is protected by original copyright rightsstatements.org