Journal
SEPARATION SCIENCE AND TECHNOLOGY
Volume 45, Issue 15, Pages 2226-2234Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/01496395.2010.507662
Keywords
ACE inhibition; -lactoglobulin; hydrolysate; ion exchanger; Protease N oAmanoo
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The aim of this work is to develop an integrative process based on the use of an ion exchange resin for the enzymatic hydrolysis of -lactoglobulin to produce peptides with angiotensin converting enzyme (ACE) inhibitory activity using whey as a feed stock. Unlike the conventional methods, the main advantage of this approach is that by integrating the selective separation of -lactoglobulin from whey and its hydrolysis less complex mixtures of peptides are produced. Furthermore, peptides of similar charge as -lactoglobulin remain adsorbed achieving further purification. In this work, the enzyme protease N Amano at an enzyme to substrate ratio of 1/100 (wt/wt) was added directly to the adsorbed proteins in a thermostatically controlled membrane reactor operated in batch mode. Separation of the smaller peptides from the enzyme and larger peptides was achieved with a 1kDa molecular weight cut-off ultrafiltration membrane. Also, this step enables the recycling of non-hydrolyzed substrates, large peptides, and enzyme. The adsorbed protein was re-solubilised in a 10mM potassium phosphate buffer (pH 7 and 45 degrees C). The different fractions were assayed for their bioactivity in terms of angiotensin converting enzyme inhibition percentage (ACEi%) and IC50 which is the concentration of peptides that can inhibit the ACE activity by 50%. Results show that permeates of 2 and 6hrs hydrolysis have the highest bioactivity with IC50=67 and 98 mu g/ml respectively.
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