Hydrolysates with emulsifying properties prepared from protein wastes using microbial protease.

Plant-based protein hydrolysates have found applications in food industry for emulsification, foaming, and increasing shelf life of food products. The objective of this study is to isolate protease-secreting bacteria hydrolyzing protein waste, and subjecting the resultant hydrolysates for the characterization for application in the food industry. Peanut cake hydrolysates were prepared using proteases from two microorganisms selected for the purpose, viz., Aneurinibacillus migulanus, VITPM11 and Aneurinibacillus aneurinilyticus, VITPS07. The cleavage specificity of the proteases from VITPM11 and VITPS07 were found to be like plasmin and elastase respectively. The cleaving sites of proteases for peanut proteins were predicted using expasy tool. The protease of VITPM11 had maximal activity of 325.8 ± 0.1 U/mL in peanut-cake media. The degree of hydrolysis (32.03 ± 0.89%), solubility (88.5 ± 1.18%), emulsion stability index (89.76 ± 2.80) and foaming stability (68.67 ± 1.53%) properties of VITPM11 protease correlated well with results from bioinformatic studies. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10068-023-01490-z.