期刊文献+

MTGase聚合大豆蛋白及其改性机理.(II)MTGase聚合改性大豆蛋白研究 被引量:16

Polymerization of Soybean Proteins and Its Modification Mechanisms by MTGase (II) Study on Polymerization Modification of Soybean Proteins by MTGase
在线阅读 下载PDF
导出
摘要 研究了微生物转谷氨酰胺酶 (MTGase)聚合作用对大豆酸沉蛋白 (SAPP)的溶解性能、乳化及起泡性能、凝胶性以及持水性能等功能特性的影响。结果显示 :1)显著地提高了SAPP对pH的稳定性 ,MTGase催化SAPP(1% )聚合 4h可获得较好的pH稳定性 ,然而降低了SAPP的溶解性能 (除等电点附近有点增加之外 ) ;2 )降低了SAPP的乳化能力 ,然而其乳化稳定性稍有增加 ;3)对SAPP的起泡能力影响不大 ,然而可显著地改善泡沫稳定性 ,SAPP经MTGase聚合 2h的样品泡沫稳定性最佳 ;4 )显著地提高SAPP的凝胶性能 ;5 )DSC分析结果表明 ,MTGase显著地提高SAPP的热变性温度 ,或者显著地改善SAPP的水化性能。 The effects of polymerization by microbial tranglutaminase (MTGase) on functionalities of soybean acid-precipitated proteins (SAPP), such as solubility, emulsifying and foaming properties, and water-holding properties were investigated. It was indicated by the results as follows: 1) The pH-stability of SAPP was remarkably improved by polymerization, and the optimal pH-stability was obtained when the SAPP (1%) was polymerized by MTGase for 4h, but the solubility of SAPP declined (except at near isoelectric point). 2) The emulsifying capacity of SAPP was reduced, while its emulsifying stability increased slightly. 3) The foaming capacity of SAPP was almost not affected by MTGase, but the foam stability was improved observably, and the optimal foam stability was obtained when SAPP was polymerized by MTGase for 2h. 4) The gel-forming property of SAPP was improved remarkably. 5) The results of DSC indicated that the thermal temperature of SAPP was improved, or the water-holding property was improved remarkably.
出处 《中国粮油学报》 EI CAS CSCD 北大核心 2004年第2期66-71,共6页 Journal of the Chinese Cereals and Oils Association
基金 广东省"十五"农产品加重大专项 (A2 0 30 1 ) 华南理工大学自然科学基金 (E52 760 )资助
关键词 微生物转谷氨酰胺酶 改性机理 聚合作用 大豆酸沉蛋白 功能特性 microbial transgltutaminase (MTGase),soybean acid-precipitated proteins (SAPP), polymerization,modification
  • 相关文献

参考文献13

  • 1Motoki M, et al. Functional properties of food proteins polymerized by transglutaminase. Agric. Biol. Chem. 1984, 48(5):1257-1261
  • 2Aluko RE and Yada RY. Effect of a microbial calcium-independent transglutaminase on functional properties of a partially purified cowpea (Vigna unguiculata) globulin. J. Sci. Food Agric. 1999, 79:286-290
  • 3Pearce KN, et al. Emulsifying properties of proteins: evaluation of a turbidietric technique. J. Agric. Food Chem. 1978, 26:716-723
  • 4Puski G. Modification of functional properties of soy proteins by proteolytic enzyme treatment. Cereal Chem. 1975, 52:655-664
  • 5Motoki M, et al. Functional properties of food proteins polymerized by transglutaminase. Agric. Biol. Chem. 1984, 48(5):1257-1261
  • 6Nio N, et al. Gelation of casein and soybean globulins by transglutaminase. Agric. Biol. Chem. 1985, 49(8):2283-2286
  • 7Renkema MS, et al. The effect of pH on heat denaturation and gel forming properties of soy proteins. J. Biotechnol. 2000, 79:223-230
  • 8Nio N, et al. Gelation mechanism of protein solution by transglutaminase. Agric. Biol. Chem. 1986, 50(4):85-855
  • 9Aluko P and Yada R. Effect of a microbial calcium-independent transglutaminase on functional properties of a partilaaly purified cowpea 9vigna unguiculata) globulin. J. Sci. Food Agric. 1999, 79:286-290
  • 10Rouilly A, et al. DSC study on the thermal properties of sunflower proteins according to their water content. Polymer. 2001, 42:10111-10117

二级参考文献1

  • 1A. -M. Hermansson. Methods of studying functional characteristics of vegetable proteins[J] 1979,Journal of the American Oil Chemists’ Society(3):272~279

共引文献50

同被引文献259

引证文献16

二级引证文献128

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部