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dc.contributor.authorHernández-Andrés, Aranzazu-
dc.contributor.authorGómez Guillén, M. C.-
dc.contributor.authorMontero García, Pilar-
dc.contributor.authorPérez-Mateos, Miriam-
dc.date.accessioned2009-10-20T07:53:45Z-
dc.date.available2009-10-20T07:53:45Z-
dc.date.issued2005-
dc.identifier.citationJournal of Food Science 70(4): C239-C245 (2005)en_US
dc.identifier.issn0022-1147-
dc.identifier.urihttp://hdl.handle.net/10261/17786-
dc.description7 pages, 5 figures.en_US
dc.description.abstractOptimal conditions for proteolytic activity in both nonpressurized and pressurized (300 MPa, 7°C, 20 min) squid (Todaropsis eblanae) muscle occurred at acid pH levels (pH 3) over a broad range of temperatures. Pressure treatment did not modify optimal pH and temperatures but did increase proteolytic activity. The acid cysteine proteases, and to a lesser extent the acid serine proteases, were the enzymes mainly affected by the high-pressure treatment. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was indicative of increased protein hydrolysis by pressurization. Myosin heavy chain in both nonpressurized and pressurized squid was degraded at all the temperatures tested, but actin was susceptible only to proteolysis in the pressure-treated muscle at 7°C and 40°C. This behavior was not observed at 55°C.en_US
dc.description.sponsorshipThis research was supported by the Spanish Comisión Internacional de Ciencia y Tecnología mainly under project ALI AGL2000-1497.en_US
dc.format.extent259768 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherInstitute of Food Technologistsen_US
dc.publisherBlackwell Publishing-
dc.relation.isversionofPostprint-
dc.rightsopenAccessen_US
dc.subjectSquiden_US
dc.subjectHigh pressureen_US
dc.subjectProteolysisen_US
dc.subjectProtease inhibitorsen_US
dc.titlePartial characterization of protease activity in squid (Todaropsis eblanae) mantle: Modification by high-pressure treatmenten_US
dc.typeartículoen_US
dc.identifier.doi10.1111/j.1365-2621.2005.tb07166.x-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttps://doi.org/10.1111/j.1365-2621.2005.tb07166.xen_US
dc.contributor.funderComisión Interministerial de Ciencia y Tecnología, CICYT (España)-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100007273es_ES
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