著者
Rino Nakamura Manami Saito Mika Maruyama Shinta Yamanaka Takahiro Tanemura Masaki Watanabe Fumiyasu Fukumori Kiyoshi Hayashi
出版者
Japanese Society for Food Science and Technology
雑誌
Food Science and Technology Research (ISSN:13446606)
巻号頁・発行日
pp.FSTR-D-22-00110, (Released:2022-10-28)
被引用文献数
1

An aminopeptidase was purified from Proteax, a food-grade commercial enzyme reagent derived from Aspergillus oryzae that showed the highest debittering effect on casein hydrolysates among nine such reagents, and its enzymatic characteristics and debittering activities were investigated. Treatment with the enzyme, identified as leucine aminopeptidase A (LapA), on pepsin-degraded casein and cod protein solutions reduced their bitterness and increased the amount of free hydrophobic amino acids such as leucine, valine, isoleucine, and phenylalanine, as well as arginine, tyrosine, and threonine. These results indicated that LapA preferentially released hydrophobic amino acid residues at the amino terminus of peptides including bitter-tasting peptides and reduced the bitterness of protein hydrolysates.