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Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/19270
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dc.contributor.authorGupta, Bhupender S.pt
dc.contributor.authorTaha, Mohamedpt
dc.contributor.authorLee, Ming-Jerpt
dc.date.accessioned2017-12-07T19:06:56Z-
dc.date.available2017-12-07T19:06:56Z-
dc.date.issued2014pt
dc.identifier.issn2046-2069pt
dc.identifier.urihttp://hdl.handle.net/10773/19270-
dc.description.abstractBiological buffers are always considered as non-toxic, biocompatible and green compounds. Therefore, we analyzed the catalytic activity of a commercial enzyme alpha-chymotrypsin (alpha-CT) in aqueous solutions of some common biological buffers (TRIS, TES, TAPS, and TAPSO) at pH 8 and T = 25 degrees C. It is found that the increase of the buffer concentration enhanced the catalytic activity of enzyme alpha-CT, and the tendency follows the order of TRIS > TES > TAPS > TAPSO. Especially in the presence of TRIS, the catalytic activity enhanced 5.5 fold.pt
dc.language.isoengpt
dc.publisherROYAL SOC CHEMISTRYpt
dc.relationinfo:eu-repo/grantAgreement/FCT/COMPETE/132936/PTpt
dc.rightsopenAccesspor
dc.subjectBOVINE SERUM-ALBUMINpt
dc.subjectIONIC LIQUIDSpt
dc.subjectORGANIC MEDIApt
dc.subjectWATERpt
dc.subjectSTABILITYpt
dc.subjectENZYMEpt
dc.subjectFLUORESCENCEpt
dc.subjectSTABILIZATIONpt
dc.subjectCOMPLEXESpt
dc.subjectPROTEINSpt
dc.titleSuperactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutionspt
dc.typearticlept
dc.peerreviewedyespt
ua.distributioninternationalpt
degois.publication.firstPage51111pt
degois.publication.issue93pt
degois.publication.lastPage51116pt
degois.publication.titleRSC ADVANCESpt
degois.publication.volume4pt
dc.relation.publisherversion10.1039/c4ra09434dpt
dc.identifier.doi10.1039/c4ra09434dpt
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