Journal of South China University of Technology (Natural Science Edition) ›› 2010, Vol. 38 ›› Issue (8): 95-99,136.doi: 10.3969/j.issn.1000-565X.2010.08.018

• Food Science & Technology • Previous Articles     Next Articles

Emulsifying Properties of Cross-Linking Product of Peanut Protein Isolate and Decapterus maruadsi Protein Hydrolysate by Transglutaminase Treatment

Hu Xiao  Zhao Mou-ming  Ren Jiao-yan  Cui Chun   

  1. School of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, Guangdong, China
  • Received:2009-11-02 Revised:2010-01-07 Online:2010-08-25 Published:2010-08-25
  • Contact: 赵谋明（1964-），男，教授，博士生导师，主要从事食品生物技术、蛋白质化学与工程、海洋资源综合利用等的研究．E-mail：femmzhao@scut．edu．cn E-mail:hnhuxiao@163．com
  • About author:胡晓（1981-），男，博士生，主要从事食品生物技术研究．
  • Supported by:

    国家自然科学基金资助项目（20676044）;国家“863”计划项目（2006AA10326）

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Abstract:

Peanut protein isolate （PPI） was cross-linked with Decapterus maruadsi protein hydralysate （DPH） under the catalyzing of transglutaminase （TGase）, and oil-in-water emulsions of the samples were prepared via the high-pressure homogenization. Then, the effects of the cross-linking on the particle size distribution, the mean diameter per particle surface area, the microstructure and the centrifugal creaming rate of the emulsions were analyzed. The results indicate that （1） TGase accelerates the linkage between PPI and DPH with different hydrolysis degrees; （2） in the electrophoretograms of the cross-linked samples, the subunit bands with low molecular mass （ 14 -31 ku） disappear while the bands with high molecular mass （ more than 97 ku） appear; （3） the hydrolysis degree of DPH greatly improves the emulsifying properties of PPI-DPH, especially at a value of 5.5% ; and （4） the TGase cross-linking improves the emulsifying activity and emulsion stability of the cross-linked PPI-DPH.

Key words: transglutaminase, peanut protein isolate, Decapterus maruadsi, cross-linking, emulsifying property