食品科学 ›› 2019, Vol. 40 ›› Issue (19): 120-127.doi: 10.7506/spkx1002-6630-20181008-052

• 基础研究 • 上一篇    下一篇

超声-转谷氨酰胺酶改善红豆蛋白功能性质及结构

赵城彬,尹欢欢,刘景圣,许秀颖,张浩,吴玉柱,曹勇,齐宝坤,吴非   

  1. (1.吉林农业大学食品科学与工程学院,小麦和玉米深加工国家工程实验室,吉林 长春 130118;2.东北农业大学食品学院,黑龙江 哈尔滨 150030)
  • 出版日期:2019-10-15 发布日期:2019-10-25
  • 基金资助:
    吉林省科技发展计划项目(20190103121JH);吉林省教育厅科学研究项目(JJKH20180654KJ)

Functional Properties and Structure of Red Bean Protein Improved by Combined Ultrasound-Transglutaminase Treatment

ZHAO Chengbin, YIN Huanhuan, LIU Jingsheng, XU Xiuying, ZHANG Hao, WU Yuzhu, CAO Yong, QI Baokun, WU Fei   

  1. (1. National Engineering Laboratory for Wheat and Corn Deep Processing, College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China; 2. School of Food Science, Northeast Agricultural University, Harbin 150030, China)
  • Online:2019-10-15 Published:2019-10-25

摘要: 采用超声联合转谷氨酰胺酶(transglutaminase,TG)处理红豆分离蛋白(red bean protein isolate,RBPI),对其功能性质和结构特征进行分析,以探究其结构修饰与功能性质的构效关系。结果表明:超声处理5 min能够使RBPI的乳化活性和发泡能力提高,但会降低泡沫稳定性,对乳液稳定性没有显著影响,同时增加表面疏水性和游离巯基含量;TG能够提高RBPI的乳化活性、乳化稳定性及泡沫稳定性,但会降低发泡能力、表面疏水性和游离巯基含量;超声-TG联合处理的RBPI具有更高的乳化活性和泡沫稳定性,更低的表面疏水性和游离巯基含量,且酰胺Ⅰ带处吸收峰强度增加,更多的无规卷曲结构转变为有序的β-折叠结构,这可能是导致RBPI功能性质改善的原因。超声处理5 min联合TG诱导的蛋白凝胶具有更加均匀、致密的微观结构,且凝胶硬度和黏附力增加,脱水收缩作用降低;峰值温度(Tp)和热焓变(ΔH)显著增加(P<0.05),改善了RBPI的热稳定性或三级结构稳定性。以上结果表明RBPI经过超声处理后更利于TG对蛋白质的交联作用,超声-TG联合处理促进了蛋白质功能性质的发挥。

关键词: 超声, 转谷氨酰胺酶, 红豆蛋白, 功能性质, 结构

Abstract: Red bean protein isolate (RBPI) was treated by ultrasound (US) combined with transglutaminase (TG), and analyzed for functional and structural characteristics. The relationship between structural modification and functional properties was explored. The results indicated that 5-min US treatment alone could improve the emulsifying activity and foaming ability of RBPI, but reduce the foam stability without affecting the emulsion stability, and it could also increase the surface hydrophobicity (H0) and free sulfhydryl content. TG alone was able to improve the emulsifying activity, emulsion stability and foam stability, but reduce foaming ability, H0 and free sulfhydryl content of RBPI. RBPI treated by US-TG had higher emulsifying activity and foam stability, and lower H0 and free sulfhydryl content. The gel induced by TG after US treatment for 5 min had a more uniform and compact microstructure with lower syneresis, and possessed increased hardness and adhesiveness. The absorption peak strength in the amide I band of RBPI treated by US-TG was enhanced, and more random coil structure was transformed into an ordered β-sheet structure, which may contribute to the improvement of functional properties. Treatment with US for 5 min combined with TG could significantly increase the peak temperature (Tp) and enthalpy (ΔH) (P < 0.05), thereby improving the thermal stability or tertiary structure stability of RBPI, which indicated that TG-induced cross-linking of RBPI was promoted by treatment with US and the combined treatment could facilitate the development of functional properties of proteins.

Key words: ultrasound, transglutaminase, red bean protein, functional properties, structure

中图分类号: