Debittering effect of Monascus carboxypeptidase during the hydrolysis of soybean protein.
The actions of pepsin and the admixture of pepsin and Monascus pilosus carboxypeptidase 1 (MpiCP-1) on the hydrolysis of soybean protein were studied. The results showed that the pepsin hydrolyzate of soybean protein was much more bitter and contained relatively smaller amounts of total free amino acids than the hydrolyzate obtained with the admixture of pepsin and MpiCP-1. In addition, hydrophilic and hydrophobic amino acids were present in almost equal proportions in the pepsin hydrolyzate, while mainly hydrophobic amino acids made up the hydrolyzate obtained with the admixture of pepsin and MpiCP-1. These results suggest that MpiCP-1 suppresses and reverses the development of the bitterness taste that results from the pepsin hydrolysis of soybean protein by releasing mainly hydrophobic amino acids from the C-termini of the bitter components.
Liu
Fang
F
Department of Food Science and Engineering, Faculty of Life Science and Technology, Central South Forestry University, Changsha, Hunan, China. Liuxfang@yahoo.com
Yasuda
Masaaki
M
D002268:Carboxypeptidases / Q000378:metabolism*; D006868:Hydrolysis / Q000187:drug effects; D032741:Monascus / Q000201:enzymology*; D010434:Pepsin A / Q000494:pharmacology; D030262:Soybean Proteins / Q000378:metabolism*
D030262:Soybean Proteins; D002268:Carboxypeptidases; D010434:Pepsin A