Reduction in the bitterness of protein hydrolysates by an aminopeptidase from <i>Aspergillus oryzae</i>

DOI Web Site 参考文献18件
  • Nakamura Rino
    Graduate School of Food and Nutritional Sciences, Toyo University
  • Saito Manami
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Maruyama Mika
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Yamanaka Shinta
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Tanemura Takahiro
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Watanabe Masaki
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Fukumori Fumiyasu
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University
  • Hayashi Kiyoshi
    Department of Food and Life Sciences, Faculty of Food and Nutritional Sciences, Toyo University

抄録

<p>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.</p>

収録刊行物

参考文献 (18)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ