SOME PROPERTIES OF ENDOGENOUS α-AMYLASE INHIBITOR FROM WHEAT GRAIN

Authors

  • Aidar Atymtaevich Khakimzhanov
  • Dinara Aitpaevna Shansharova
  • Lyazzat Bekenovna Umiraliyeva
  • Luděk HÅ™ivna
  • Viera Å ottníková
  • Saltanat Kadenovna Madenova
  • Diana Bayshagylovna Abdraimova

Keywords:

α-amylase, isoenzymes, subtilisin, inhibitor, wheat

Abstract

The 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 90° C for 10 minutes. The protein is localized in the peripheral parts of the seed, and in the starchy endosperm.

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Published

2014-02-01

How to Cite

Atymtaevich Khakimzhanov, A., Aitpaevna Shansharova, D., Bekenovna Umiraliyeva, L., HÅ™ivna, L., Å ottníková, V., Kadenovna Madenova, S., & Bayshagylovna Abdraimova, D. (2014). SOME PROPERTIES OF ENDOGENOUS α-AMYLASE INHIBITOR FROM WHEAT GRAIN. Journal of Microbiology, Biotechnology and Food Sciences, 3(special issue 3 (Food Sciences), 241–243. Retrieved from https://office2.jmbfs.org/index.php/JMBFS/article/view/7583

Issue

Vol. 3 No. special issue 3 (Food Sciences) (2014): February

Section

Food Sciences

License

Copyright (c) 2014 Aidar Atymtaevich Khakimzhanov, Dinara Aitpaevna Shansharova, Lyazzat Bekenovna Umiraliyeva, Luděk Hřivna, Viera Šottníková, Saltanat Kadenovna Madenova, Diana Bayshagylovna Abdraimova

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