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dc.contributor.authorKhakimzhanov, Aidar
dc.contributor.authorShansharova, Dinara
dc.contributor.authorUmiralyieva, Lyazzat
dc.contributor.authorHrivna, Ludek
dc.contributor.authorSottnikova, Viera
dc.contributor.authorMadenova, Saltanat
dc.contributor.authorAbdraimova, Diana
dc.date.accessioned2018-05-25T08:36:29Z
dc.date.available2018-05-25T08:36:29Z
dc.date.issued2014
dc.identifier.urihttp://acagor.kz:8080/xmlui/handle/123456789/28
dc.description.abstractThe protein with endogenous α - amylase inhibitor activity was extracted and purified from wheat (Triticum aestivum) grains through 70% ammonium sulphate fractionation, ion-exchange chromatography on DEAE-Sephacel and gel-chromatography on Toyapearl HW-50. the molecular weight and isoelectric point of protein were estimated about 21 kD and 7.0 respectively. The inhibitor repressed of high pI wheat α - amylase isozymes, but had no effect on amylases of microbial and animal origin. The inhibitor also exhibited activity towards serine protease subtilisin. The inhibitor was the most active at pH 7.8 to pH 8.0 and was stable up to 90C for 10 minutes. The protein is localized in the peripheral parts og the seed, and in the starchy endosperm.ru_RU
dc.language.isoenru_RU
dc.relation.ispartofseriesJournal og Microbiology, Biotechnology and Food Sciences;241-243
dc.subjectα - amylaseru_RU
dc.subjectisoenzymesru_RU
dc.subjectsubtilisinru_RU
dc.subjectinhibitorru_RU
dc.subjectwheatru_RU
dc.titleSome properties of endogenous α - Amylase inhibitor from wheat grainru_RU
dc.typeArticleru_RU


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