Abstract
In order to exploit industrial discards, protein enzymatic hydrolysis is a currently popular methodology for obtaining bioactive peptides. However, once released, most promising peptides have to be selected from the mixture. In this work, the suitability of pepsin (EC 3.4.23.1) to hydrolyse serum albumin in order to obtain bioactive peptides was assessed. Then, a suitable process to obtain best separation of bioactive peptides was evaluated, using polyethersulfone membranes at different pH values. Serum albumin was easily hydrolysed by pepsin, reaching a DH value of the 65.64 ± 1.57% of the maximum possible. A 23.25% of the identified peptides possessed high bioactivity scores (greater than 0.5), and one of them had reported bioactivity (LLL). Charge mechanisms always predominated over the sieve effect, and best transmission was accomplished at pH values close to the peptides isoelectric points. Basic and neutral peptides with the highest scores were always the most transmitted. Membrane material had greater influence than NMWCO in determining peptide transmission. In order to obtain purified fractions rich in peptides with high bioactivity scores from serum albumin, polyethersulfone membranes (applicable to industrial scale) of 5 kDa MWCO should be used at basic pH values after pepsin digestion.
Highlights
Bioactive peptides are defined as short amino acid fragments encrypted in the primary sequence of proteins that can confer health-related functions beyond basic nutritional benefits when orally administered[1]
The extent of protein hydrolysis was expressed as the degree of hydrolysis (DH), and monitored as a function of time
The DH increased with hydrolysis time
Summary
Bioactive peptides are defined as short amino acid fragments encrypted in the primary sequence of proteins that can confer health-related functions beyond basic nutritional benefits when orally administered[1]. No bibliographical evidence was found of pure BSA pepsinolysis with the purpose of obtaining bioactive peptides in which the all the hydrolysate sequences were identified, several works about WPC and WPI hydrolysis with pepsin suggest BSA as a good substrate for the enzyme. Acidic peptides were all more transmitted through the membrane with higher MWCO, with no exceptions (Average Tr of 23.47% for PES1, while 35.45% for PES5).
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