Substantial Improvement of Tryptic and Chymotryptic Hydrolysis of β-Lactoglobulin Pretreated with High Voltage Electrical Treatments

Abstract

β-lactoglobulin (β-lg) is an important source of biologically and functionally active peptides that are of particular interest in agri-food, nutraceutical, and pharmaceutical industries. Enzymatic hydrolysis of proteins remains the most common mode of peptide production. However, efficient hydrolysis of proteins and particularly β-lg is difficult to perform due to their compact globular structure. Thus, the current study deals with green high-voltage electric treatments (HVET): pulsed electric fields and electric arc to pretreat β-lg and improve its proteolysis by trypsin and chymotrypsin. The results demonstrate substantial improvement of hydrolysis performance after the pretreatment of β-lg with HVET compared to the non-pretreated and preheated β-lg. Moreover, HVET led to the peptide release from β-lg even before the addition of proteases. Furthermore, pioneer studies of proteolysis kinetics and structural changes of β-lg molecules subjected to HVET allowed a better understanding of the mechanisms underlying hydrolysis improvement.

Enzymatic Hydrolysis of Water Lentil (Duckweed): An Emerging Source of Proteins for the Production of Antihypertensive Fractions

“…It has 112 theoretical cleavage sites for this protein, which is consistent with the rather high DH. Chymotrypsin, on the other hand, cleaves the C-terminal side of aromatic amino acids, leucine and methionine [59]. It presents 100 theoretical cleavage sites within the protein (slightly less than pepsin), corroborating the slightly lower DH observed.…”

“…This observation implied that papain tends to target RuBisCO proteins more than others, leading to a high number of cleavage sites within this protein and yielding to a low DH at the same time. Trypsin, distinguished by its high specificity, cleaves on the carboxyl side of lysine or arginine, unless succeeded by proline [59]. This results in 48 theoretical cleavage sites within the protein, seemingly contradicting the high DH.…”

Terrestrial Compound Protein Replacing Dietary Fishmeal Improved Digestive Enzyme Activity, Immune Response, Intestinal Microflora Composition, and Protein Metabolism of Golden Pompano (Trachinotus ovatus)

“…Intestinal enzyme activities were considered to be a reliable indicator of the intestinal digestive and absorptive capacities of fish, due to the fact that these enzymes determine the ability of fish to obtain and utilize nutrients in diets [56][57][58][59]. CHT is a proteolytic enzyme secreted by the pancreas, which can rapidly break down denatured proteins [60]. In this study, the activity of CHT in the foregut of the CP80 group was similar to that of the FM30 group, but lower than that of the AP80 and PP80 groups, possibly due to the fact that the meat and bone meal in AP80 diet contains bones that are difficult to digest [46], while the PP80 diet has a high content of anti-nutritional factors [51], so it is necessary to improve the digestive enzyme activity of fish to cope with indigestible substances.…”

Electrodialysis Processes an Answer to Industrial Sustainability: Toward the Concept of Eco-Circular Economy?—A Review

“…It can also be difficult to access this data for industrial processes where it is often kept confidential. However, it is possible to use a simplified approach to assess eco-efficiency that uses environmental impact indicators instead of environmental impact scores determined by an LCA [ 39 , 40 , 41 ] ( Table 1 ). These indicators, determined by an analysis of the process, are linked to inputs or outputs contributing significantly to the environmental impact (e.g., energy consumption, water consumption, etc.).…”