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BACKGROUND
Various neutral and alkaline peptidases are commercially available for use in protein hydrolysis under neutral to alkaline conditions. However, the hydrolysis of proteins under acidic conditions by applying fungal aspartic peptidases (FAPs) has not been investigated in depth so far. The aim of this study, thus, was to purify a FAP from the commercial enzyme preparation, ROHALASE® BXL, determine its biochemical characteristics, and investigate its application for the hydrolysis of food and animal feed proteins under acidic conditions.
RESULTS
A Trichoderma reesei derived FAP, with an apparent molecular mass of 45.8 kDa (sodium dodecyl sulfate–polyacrylamide gel electrophoresis; SDS-PAGE) was purified 13.8-fold with a yield of 37% from ROHALASE® BXL. The FAP was identified as an aspartate protease (UniProt ID: G0R8T0) by inhibition and nano-LC-ESI-MS/MS studies. The FAP showed the highest activity at 50°C and pH 4.0. Monovalent cations, organic solvents, and reducing agents were tolerated well by the FAP. The FAP underwent an apparent competitive product inhibition by soy protein hydrolysate and whey protein hydrolysate with apparent Ki-values of 1.75 and 30.2 mg*mL−1, respectively. The FAP showed promising results in food (soy protein isolate and whey protein isolate) and animal feed protein hydrolyses. For the latter, an increase in the soluble protein content of 109% was noted after 30 min.
CONCLUSION
Our results demonstrate the applicability of fungal aspartic endopeptidases in the food and animal feed industry. Efficient protein hydrolysis of industrially relevant substrates such as acidic whey or animal feed proteins could be conducted by applying fungal aspartic peptidases. © 2022 Society of Chemical Industry.
This review provides an overview on the production and analysis techniques of antioxidative peptides from food proteins. Regarding the production of antioxidative peptides, interlinked factors must be considered. Depending on the protein substrate, different peptidases or peptidase systems containing multiple enzymes as well as a specific production process must be chosen. The antioxidative peptides might be produced in a batch process including multiple pre- and post-treatments, besides the hydrolyses with peptidases itself. As an alternative, the potential of continuous production systems is discussed in this review. Furthermore, robust analyses tools are needed to gain control of the process and final product properties. With no standardized methodology available for antioxidative peptide evaluation, pros and cons of various strategies for peptide separation and antioxidative measurement are discussed in this review. Therefore, this review provides a roadmap for antioxidative peptide generation from various sources for research and development as well as for potential industrial use.