期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 52, 期 6, 页码 1564-1571出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf034813t
关键词
soybean proteins; high-pressure treatment; protein structure; protein denaturation; protein aggregation
Changes induced by high pressure (HP) treatment (200-600 MPa) on soybean protein isolates (SP1) at pH 3 (SP13) and pH 8 (SP18) were analyzed. Changes in protein solubility, surface hydrophobicity (Ho), and free sulfhydryl content (SHF) were determined. Protein aggregation and denaturation and changes in secondary structure were also studied. An increase in protein Ho and aggregation, a reduction of free SH, and a partial unfolding of 7S and 11S fractions were observed in HP-treated SP18. Changes in secondary structure were also detected, which led to a more disordered structure. HP-treated SP13 was partially denatured and presented insoluble aggregates. A major molecular unfolding, a decrease of thermal stability, and an increase of protein solubility and Ho were also detected. At 400 and 600 MPa, a decrease of the SHF and a total denaturation were observed.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据