Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions
文献类型: 外文期刊
第一作者: Feng, Xiao-Long
作者: Feng, Xiao-Long;Liu, Hong-Zhi;Shi, Ai-Min;Liu, Li;Wang, Qiang;Adhikari, Benu
作者机构:
关键词: Arachin;Conarachin;Peanut protein;Transglutaminase crosslinking;Physicochemical properties
期刊名称:FOOD RESEARCH INTERNATIONAL ( 影响因子:6.475; 五年影响因子:6.508 )
ISSN: 0963-9969
年卷期: 2014 年 62 卷
页码:
收录情况: SCI
摘要: Arachin and conarachin-rich fractions of peanut protein were extracted by using cryoprecipitation followed by centrifugation. These two fractions were individually crosslinked using transglutaminase (TG). The physicochemical characteristics including aggregation due to crosslinking, solubility, thermal denaturation temperature (T-d) and denaturation enthalpy (Delta H), morphology of microstructure and surface hydrophobicity (H-0) of TG-treated and untreated arachin and conarachin-rich fractions were determined. The relative contents of arachin and conarachin in arachin and conarachin-rich fractions were 75% and 65%, respectively. Conarachin-rich fractions were found to more conveniently aggregate than arachin-rich from the results of SDS-PAGE. The solubility of treated arachin and conarachin-rich fractions was decreased by 66.13% and 36.91%, respectively. Only marginal increase in T-d was observed in the case of crosslinked arachin-rich fraction while significant increase in T-d (of the order of 10 degrees C) was observed in crosslinked conarachin-rich fraction. The H-0 values of both crosslinked arachin and conarachin-rich fractions decreased significantly. The treated arachin and conarachin-rich fractions had more compact microstructure compared to their untreated samples. Hence, the comparison of arachin and conarachin-rich in crosslinking and the mechanism of properties enhancement by TG is the aim of the research. (C) 2014 Elsevier Ltd. All rights reserved.
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