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

Area of Science:

• Food Science
• Microbiology
• Biotechnology

Background:

• Plant-based protein hydrolysates are valuable food ingredients.
• Enzymatic hydrolysis using microbial proteases offers a sustainable method for producing these hydrolysates.
• Peanut cake is an underutilized protein-rich byproduct.

Purpose of the Study:

• To isolate protease-secreting bacteria capable of hydrolyzing protein waste.
• To characterize peanut cake hydrolysates produced by selected bacterial proteases for food industry applications.

Main Methods:

• Isolation and selection of protease-secreting bacteria (*Aneurinibacillus migulanus* VITPM11 and *Aneurinibacillus aneurinilyticus* VITPS07).
• Preparation of peanut cake hydrolysates using bacterial proteases.
• Characterization of protease activity, cleavage specificity (plasmin-like, elastase-like), and hydrolysate properties (degree of hydrolysis, solubility, emulsion stability, foaming stability).
• Bioinformatic prediction of protease cleavage sites using expasy tool.

Main Results:

• Protease from *Aneurinibacillus migulanus* VITPM11 exhibited maximal activity (325.8 U/mL) and demonstrated properties suitable for food applications.
• The VITPM11 protease showed high degree of hydrolysis (32.03%), solubility (88.5%), emulsion stability (89.76%), and foaming stability (68.67%).
• Cleavage specificity of VITPM11 protease was predicted to be similar to plasmin, and VITPS07 similar to elastase.

Conclusions:

• Bacterial proteases, particularly from *Aneurinibacillus migulanus* VITPM11, are effective in hydrolyzing peanut cake proteins.
• The resulting hydrolysates possess favorable functional properties, indicating their potential for use in the food industry.
• Bioinformatic analysis supports the experimental findings on protease activity and cleavage sites.