Changes of alanyl aminopeptidase activity and free amino acid contents in biceps femoris during processing of Jinhua ham

被引:65
作者
Zhao, GM
Zhou, GH [1 ]
Tian, W
Xu, XL
Wang, YL
Luo, X
机构
[1] Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Peoples R China
[2] Henan Agr Univ, Coll Food Sci & Technol, Zhengzhou 450002, Peoples R China
[3] Henan Agr Univ, Coll Vet & Anim Sci, Zhengzhou 450002, Peoples R China
[4] Henan Agr Univ, Univ Ctr Lab, Zhengzhou 450002, Peoples R China
关键词
Jinhua ham; aminopeptidase; alanyl aminopeptidase; free amino acid; response surface methodology;
D O I
10.1016/j.meatsci.2005.05.006
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Sixty experimental Jinhua hams were processed by a traditional method. The potential alanyl aminopeptidase (AAP) activity in biceps femoris was determined. The effects of temperature, salt content, sodium nitrate content and pH on muscle AAP were evaluated using response surface methodology. Porcine muscle was found to possess very strong potential AAP activity that decreased gradually during processing from 201,63 5 U g(-1) before salting to 6147 U g(-1) after aging. Temperature, pH and salt content had significant exponential effects on AAP activity (P < 0.001). Both temperature and salt content interacted with pH in their effects on AAP activity (P < 0.01). However, 0-50 mg L-1 sodium nitrate had no detectable effect on AAP activity (P > 0.05). The regression model showed muscle AAP maintaining its activity all through Jinhua ham processing, indicating that muscle AAP may generate free amino acids during the processing and storage of Jinhua ham. The concentrations of free amino acids increased significantly (P < 0.05) during Jinhua ham processing, except for arginine and cystine. The concentrations of most free amino acids were 5-20 times higher in the final product than in hams before salting. Final concentrations exceeded thresholds for sensory detection, thus implicating an important role of free amino acids in the determination of Jinhua ham flavor. (C) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:612 / 619
页数:8
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