A rapid quantitative assay for bacterial protease activity

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dc.creatorHien, Nguyen Thi Phuoc
dc.date.accessioned2016-11-14T23:11:11Z
dc.date.available2011-02-19T00:57:33Z
dc.date.available2016-11-14T23:11:11Z
dc.date.issued2006-08
dc.degree.departmentChemistryen_US
dc.description.abstractA rapid quantitative stained hide powder assay was studied as a possible replacement for the gelatin film test, used to detect bacterial enzymes within hide juice of delayed cured hides. The ability of the method was investigated by employing different kinds of substrates and enzymes. Substrates from dogchew and rawhide were hydrolyzed by Proleather FG-F, Protex 6L and Alcalase enzyme under optimum conditions. Reproducibility of the dogchew substrate was higher but hydrolysis efficiency was less than for the rawhide substrate. To improve reproducibility and hydrolysis efficiency, a stable, neutralized stained hide powder was produced and served as a substrate for calibration. Analytical figures of merit are described. The relations between the efficiency of hydrolysis and enzyme concentration or enzyme activity were linear. The effect of salt shifted the calibration toward lower hydrolysis efficiency. The slopes did not change. The method could detect the Proleather FG-F enzyme concentration as low as 0.01 ìg/ml or enzyme activity of 1.01x10-3 LVU/ml without salt and 0.05 ìg/ml or enzyme activity of 5.05x10-3 LVU/ml with salt.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2346/22397en_US
dc.language.isoeng
dc.publisherTexas Tech Universityen_US
dc.rights.availabilityUnrestricted.
dc.subjectEnzyme acten_US
dc.subjectHide powder assayen_US
dc.subjectSalt effecten_US
dc.subjectSubstrateen_US
dc.titleA rapid quantitative assay for bacterial protease activity
dc.typeThesis

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