Utilization of blood by-products: An in silico and experimental combined study for BSA usage

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.

Thai traditional fermented fish paste Ka‐pi‐plaa : Chemical compositions and physical properties

“…The DH values were correlated with formal nitrogen and amino nitrogen contents and are shown in Table 3. DH measures the extent of cleavage of peptide linkages, and a DH value close to 100% means complete hydrolysis from protein to free amino acids (Arrutia et al, 2017). Besides, DH might be associated with the attributes in fermented products including bioactivity, taste, flavor, and others, due to the produced free amino groups, and their availability to undergo several reactions (e.g., Maillard reaction).…”

Studies on Chromatographic Fractioning by Cations Exchangers of a Bovine Hemoglobin Hydrolysate

“…If such a peptide is fractionated several times during its passage through the quadrupoles of the mass spectrometer, we noticed the occurrence of several successive peaks that allowed us to identify it [18,19].…”