Characterization of Yeast Protein Hydrolysate for Potential Application as a Feed Additive

• Published in: Food science of animal resources Vol. 44; no. 3; pp. 723 - 737
• Main Authors: Min, Ju Hyun, Lee, Yeon Ju, Kang, Hye Jee, Moon, Na Rae, Park, Yong Kuk, Joo, Seon-Tea, Jung, Young Hoon
• Format: Journal Article
• Language: English
• Published: Korea (South) Korean Society for Food Science of Animal Resources 01.05.2024; 한국축산식품학회
• Subjects: 축산학; exoprotease; endoprotease; hydrolysis; alternative protein; yeast protein
• ISSN: 2636-0772; 2636-0780; 2636-0780
• DOI: 10.5851/kosfa.2024.e33

Yeast protein can be a nutritionally suitable auxiliary protein source in livestock food. The breakdown of proteins and thereby generating high-quality peptide, typically provides nutritional benefits. Enzyme hydrolysis has been effectively uesed to generate peptides; however, studies on the potential applications of different types of enzymes to produce yeast protein hydrolysates remain limited. This study investigated the effects of endo- (alcalase and neutrase) and exotype (flavourzyme and prozyme 2000P) enzyme treatments on yeast protein. Endotype enzymes facilitate a higher hydrolysis efficiency in yeast proteins than exotype enzymes. The highest degree of hydrolysis was observed for the protein treated with neutrase, which was followed by alcalase, prozyme 2000P, and flavourzyme. Furthermore, endotype enzyme treated proteins exhibited higher solubility than their exotype counterparts. Notably, the more uniform particle size distribution was observed in endotype treated yeast protein. Moreover, compared with the original yeast protein, the enzymatic protein hydrolysates possessed a higher content of β-sheets structures, indicating their higher structural stability. Regardless of enzyme type, enzyme treated protein possessed a higher total free amino acid content including essential amino acids. Therefore, this study provides significant insights into the production of protein hydrolysates as an alternative protein material.