Debittering Mechanism in Bitter Peptides of Enzymatic Hydrolysates from Milk Casein by Aminopeptidase T |
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| Authors: | ETSUO MINAGAWA SHUICHI KAMINOGAWA FUJI TSUKASAKI KUNIO YAMAUCHI |
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| Affiliation: | Authors Minagawa, Kaminogawa, and Yamauchi are with the Dept. of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku Tokyo 113, Japan. Author Tsukasaki is with the Research &Development Dept, Yotsuba Milk Products Co. Ltd, Otofukecho, Kato-gun, Hokkaido 080, Japan. |
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| Abstract: | The bitter peptide fraction present in casein hydrolysates obtained by using three proteases (subtilisin, papain and trypsin) was treated with aminopeptidase T from Thermus aquaticus YT-1. The bitterness of the bitter peptide fraction could be decreased, and it sometimes disappeared completely, with an increase in free amino acids. The percentages of total free amino acids released from each bitter peptide fraction (subtilisin, papain and trypsin) by aminopeptidase digestion for 20 hr were approximately 11%, 8.7%, and 6.5%, respectively. Bitter peptide (αs1-CN f91-100) was isolated from a tryptic hydrolysate of casein by HPLC, its threshold value of bitterness being 2.9 ppm (w/v). The peptide (αs1-CN f96-100) obtained from the amino peptidase digestion of this bitter peptide showed no bitterness. |
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