Novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification.

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dc.contributor.authorSiddiqui, KSen_AU
dc.contributor.authorParkin, DMen_AU
dc.contributor.authorCurmi, PMGen_AU
dc.contributor.authorDe Francisci, Den_AU
dc.contributor.authorPoljak, Aen_AU
dc.contributor.authorBarrow, KDen_AU
dc.contributor.authorNoble, MHen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorCavicchioli, Ren_AU
dc.date.accessioned2009-08-20T05:30:45Zen_AU
dc.date.accessioned2010-04-30T05:04:40Zen_AU
dc.date.available2009-08-20T05:30:45Zen_AU
dc.date.available2010-04-30T05:04:40Zen_AU
dc.date.issued2009-07-01en_AU
dc.date.statistics2009-07-01en_AU
dc.description.abstractThe alkaline protease, savinase was chemically modified to enhance the productivity of the enzyme at low temperatures on a complex polymeric protein (azocasein) substrate. At 5 and 15 degrees C, savinase modified with ficol or dextran hydrolyzed fivefold more azocasein than the unmodified savinase. Kinetic studies showed that the catalytic improvements are associated with changes in uncompetitive substrate inhibition with K-i values of modified savinases sixfold higher than the unmodified savinase. Modeling of small-angle scattering data indicates that two substrate molecules bind on opposing sides of the enzyme. The combined kinetic and structural data indicate that the polysaccharide modifier sterically blocks the allosteric site and reduces substrate inhibition. In contrast to the properties of cold-active enzymes that generally manifest as low activation enthalpy and high flexibility, this study shows that increased activity and productivity at low temperature can be achieved by reducing uncompetitive substrate inhibition, and that this can be achieved using chemical modification with an enzyme in a commercial enzyme-formulation. Biotechnol. Bioeng. 2009;103: 676-686. © 2009, Wiley-Blackwell.en_AU
dc.identifier.citationSiddiqui, K. S., Parkin, D. M., Curmi, P. M. G., De Francisci, D., Poljak, A., Barrow, K., Noble, M. H., Trewhella, J., & Cavicchioli, R. (2009). Novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification. Biotechnology and Bioengineering, 103(4), 676-686. doi:10.1002/bit.22300en_AU
dc.identifier.govdoc1305en_AU
dc.identifier.issn0006-3592en_AU
dc.identifier.issue4en_AU
dc.identifier.journaltitleBiotechnology and Bioengineeringen_AU
dc.identifier.pagination676-686en_AU
dc.identifier.urihttp://dx.doi.org/10.1002/bit.22300en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1693en_AU
dc.identifier.volume103en_AU
dc.language.isoenen_AU
dc.publisherWiley-Blackwellen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectEnzymesen_AU
dc.subjectCrystal structureen_AU
dc.subjectEscherichia colien_AU
dc.subjectAmylaseen_AU
dc.subjectCatalytic effectsen_AU
dc.titleNovel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification.en_AU
dc.typeJournal Articleen_AU
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