ISOLATION AND CHARACTERIZATION OF A PANCREATIC AMYLASE INHIBITOR

Authors

DOI:

https://doi.org/10.15421/jchemtech.v30i4.263201

Keywords:

Key words: oat grain, oat flour; extraction; affinity chromatography; gel electrophoresis; pancreatic am-ylase inhibitor; molecular weight, biotechnology, pharmacy.

Abstract

The role and sources of digestive enzyme inhibitors, which are effective correctors of digestive processes in the body, are characterized. Screening of vegetable raw materials zoned in Ukraine for the content of pancreatic α-amylase inhibitors showed the expediency of using secondary raw materials – oat flour Avena sativa. An inhibitor of pancreatic amylase from oat flour has been isolated and characterized. It has significant antiamylolytic activity. The obtained inhibitor is promising for creating compositions designed for nutritional correction of increased activation of amylolytic enzymes. Grain extracts and oat flour are characterized by significant inhibitory activity to pancreatic amylase. The water-soluble protein fractions from oat grains and oat flour have the maximum inhibitory activity. The highest degree of inhibitor extraction from oat flour occurs when extracting 0.15 M NaCl in 0.1 M hydrocarbonate buffer, pH 9.2. A monomeric pancreatic amylase inhibitor with a molecular mass of 25.11 kDa was isolated by affinity chromatography with a purity of 92.7; pH-optimum 5.5, thermo-optimum 37 0C. The inhibitor is most stable at pH 5.0 and 20 0C.

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Published

2023-01-26

Issue

Vol. 30 No. 4 (2022): Journal of Chemistry and Technologies

Section

Chemical Technology

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