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Use of Different Proteases to Obtain Whey Protein Concentrate Hydrolysates with Inhibitory Activity toward Angiotensin‐Converting Enzyme
Author(s) -
Morais Harriman A.,
Silvestre Marialice P.C.,
Amorin Larissa L.,
Silva Viviane D.M.,
Silva Mauro R.,
Simões e Silva Ana Cristina,
Silveira Josianne N.
Publication year - 2014
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/jfbc.12032
Subject(s) - aspergillus oryzae , hydrolysate , bacillus licheniformis , protease , proteases , whey protein , food science , chemistry , enzyme , biochemistry , hydrolysis , papain , casein , proteolysis , biology , bacillus subtilis , bacteria , genetics
The effects of proteolytic enzyme type (including pancreatin and proteases from B acillus licheniformis, A spergillus oryzae and A . sojae ) and enzyme : substrate ratio ( E : S = 0.5:100, 1:100, 2:100, 3:100, 4:100 and 8:100) were evaluated in this work with the aim of obtaining whey protein concentrate hydrolysates with inhibitory activity toward angiotensin‐converting enzyme. Twenty‐four hydrolysates were prepared, and their inhibitory activities ( IA ) were evaluated in vitro , resulting in inhibition rates ranging from 2.02 to 96.66%. Eleven samples had IAs that were very high (>80%). The hydrolysates obtained using the B . licheniformis protease had the highest IA values at all tested E : S ratios. In some cases, lowering the E : S ratio produced a higher IA value. This was observed for the B . licheniformis protease when the ratio was lowered from 2:100 to 1:100, as well as for the A . oryzae protease when lowered from 3:100 to 2:100 and from 2:100 to 1:100. Practical Applications Whey is the most abundant protein subproduct of the dairy industry, representing about 80% of the volume of the milk. Thus, it is of great interest to create options to use whey or its isolated proteins. Among the possibilities that promote an exponential aggregated value to whey is the enzymatic hydrolysis of its proteins, since this treatment promotes the breakdown of the protein molecule into smaller units and has been outstanding in improving its nutritional, sensorial and functional properties. Also, the whey proteins have been identified as nutrients with functional activity, containing bioactive peptides able to modulate some physiological responses of either mammalian or rats. Such peptides are inactive as part of the intact proteins, but they become active when released during digestion or during in vitro enzymatic hydrolysis. In this way, whey protein hydrolysates could be introduced into the diet as an alternative and non‐pharmacological approach to prevent and treat arterial hypertension.