KINETICS OF Α-AMYLASE INHIBITION BY ALBIZIA LEBBECK SEED PROTEIN DIGESTS
Abstract
ABSTRACT
Proteins from n-hexane - treated Albizia lebbeck seed flour were isolated using alkaline solubilization followed by acid-induced precipitation. Albizia lebbeck seed proteins were hydrolyzed using the proteinases trypsin, chymotrypsin and trypsin/chymotrypsin. The resulting hydrolysates were then evaluated for α-amylase inhibitory properties and kinetics. The results revealed that Albizia lebbeck seed proteins were most susceptible to chymotrypsin hydrolysis (degree of hydrolysis of 10.32±0.92%) when compared to those of trypsin and Trypsin/Chymotrypsin, which had DH values of 3.91±0.62 % and 4.21±0.31% respectively. Kinetic data showed a competitive subtype of mixed inhibition for chymotrypsin, uncompetitive subtype of mixed inhibition for trypsin hydrolysates and an mixed mode for
Trypsin/Chymotrypsin hydrolysates, with ki, of 2.094mg/ml, 0.825mg/ml and 0.315mg/ml for chymotrypsin, trypsin and Trypsin/Chymotrypsin hydrolysates respectively. The study concludes that Albizia lebbeck seed proteins, on proteolysis with appropriate enzymes, possess potentially therapeutic peptides which can be further characterized towards the development of provide peptide-based alternatives in the management of diabetes mellitus.
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