谷氨酰胺转氨酶交联对牦牛乳曲拉酪蛋白功能性质的影响

史莹; 杨敏; 梁琪; 文鹏程; 张卫兵; 张炎

doi:10.13386/j.issn1002-0306.2014.08.031

谷氨酰胺转氨酶交联对牦牛乳曲拉酪蛋白功能性质的影响

史莹^1,2,
杨敏^2,3,
梁琪^1,2,
文鹏程^1,2,
张卫兵^1,2,
张炎^1,2

1. 甘肃农业大学食品科学与工程学院
2. 甘肃省功能乳品工程实验室
3. 甘肃农业大学理学院

基金项目:

国家自然科学基金资助项目(30960260)；

详细信息

作者简介:
史莹 (1988-) , 女, 在读硕士研究生, 研究方向:乳品科学与技术。;

中图分类号: TS252.1
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- 文章访问数: 153
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出版历程
- 收稿日期: 2013-08-04

Effect of transglutaminase cross-linking on the functional properties of kurut casein from yak milk

College of Food Science and Engineering, Gansu Agricultural University
Functional Dairy Product Engineering Lab of Gansu
College of Science, Gansu Agricultural University

摘要

摘要: 以曲拉和荷斯坦牛乳酪蛋白为原料,利用安全、高效的谷氨酰胺转氨酶对其进行交联修饰,研究谷氨酰胺转氨酶对酪蛋白功能性质的影响,测定交联前后样品的持水性、持油性、热稳定性、黏度、起泡性。结果表明,牦牛乳曲拉酪蛋白和荷斯坦牛乳酪蛋白经过谷氨酰胺转氨酶交联后,两种酪蛋白的交联度分别可达到20.04%(p<0.05)和25.15%(p<0.05),曲拉酪蛋白的持水性、热稳定性、黏度和泡沫稳定性显著增加(p<0.05),荷斯坦酪蛋白的黏度和热稳定性显著增加(p<0.05),其余性质均无显著差异。研究结果能为酶法改性酪蛋白的工业化生产提供理论依据。
- 谷氨酰胺转氨酶 /
- 酪蛋白 /
- 交联 /
- 功能性质
Abstract: Kurut caseins and cow caseins as the research object were modified with safe and effective transglutaminase. Effcet of transglutaminase cross- linking on the functional properties of casein were investigated. Water-holding capacity, fat-binding capacity, heat stability, viscosity and foaming properties were measured in this study. The results showed that the free amino groups of kurut caseins and cow caseins respectively decrease by 20.04% (p<0.05) and 25.15% (p<0.05) after transglutaminase cross-linking. Waterholding capacity, heat stability, viscosity and foam stability of kurut caseins significantly increased (p<0.05) .Viscosity and heat stability of cow caseins significantly increased (p <0.05) . The other properties was no obvious different. The results provided theoretical basis for industrial production of enzymatic modification with casein.
- transglutaminase /
- casein /
- cross-linking /
- functional properties

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参考文献(20)

[1]	Cui L, Fan X R, Wang P, et al.Casein and transglutaminasemediated modification of wool surface[J].English Life Science, 2011, 11 (2) :201-206.
[2]	甘伯中, 常海军, 余群力, 等.牦牛曲拉干酪素脱色工艺优化[J].农业工程学报, 2006, 22 (10) :203-207.
[3]	Mao X Y, Cheng X, Wang X.Free-radical-scavenging and anti-anflammatory effort of yak milk casein before and after enzymatic hydrolysis[J].Food Chemistry, 2011, 126 (2) :484-490.
[4]	Wang P J, Liu H N, Wen P C, et al.The composition, size and hydration of yak casein micelles[J].International Dairy Journal, 2013, 31 (2) :107-110.
[5]	Nahid A A, Salma H A, ElShazali A M, et al.Effect of Transglutaminase Cross Linking on the Functional Properties as a Function of NaCl Concentration of Legumes Protein Isolate[J].International Journal of Biological and Life Sciences, 2010, 6 (1) :8-13.
[6]	Flanagan J, FitzGerald R J.Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre-and post-hydrolysis[J].International Dairy Journal, 2003, 13 (2-3) :135-143.
[7]	Elvan魻.The use of transglutaminase in dairy products[J].International Journal of Dairy Technology, 2006, 59 (1) :1-7.
[8]	Babiker F E E, Khan M A S, Naotoshi M, et al.Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties[J].Food Research International, 1996, 29 (7) :627-634.
[9]	Siu N C, Ma C Y, Mock W Y, et al.Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase[J].Journal Agricultural and Food Chemical, 2002, 50 (9) :2666-2672.
[10]	O’Sullivan M M, Kelly A L, Fox P F.Influence of transglutaminase treatment on some physico-chemical properties of milk[J].Dairy Research, 2002, 69 (3) :433-442.
[11]	Caterina D, Maria T G, Rocco R, et al.Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein[J].Food Chemistry, 2002, 78 (3) :363-368.
[12]	Tomotake H, Shimaoka I, Kayashita J, et al.Physicochemical and Functional Properties of Buckwheat Protein Product[J].Journal of Agricultural and Food Chemistry, 2002, 50 (7) :2125-2129.
[13]	Zheng H G, Yang X Q, Tang C H, et al.Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties[J].Food Research International, 2008, 41 (2) :154-164.
[14]	Jiang S J, Zhao X H.Transglutaminase-induced crosslinking and glucosamine conjugation of casein and some functional properties of the modified product[J].International Dairy Journal, 2011, 21 (4) :198-205.
[15]	Christopher P W, Debra A C, Valentineval W, et al.Immobilization and Utilization of the Recombinant Fusion Proteins Trypsin-Streptavidin andStreptavidin-Transglutaminase for Modification of Whey Protein Isolate Functionality[J].Agric Food Chem, 2002, 50 (13) :3723-3730.
[16]	Ahn H J, Kim J H, Ng P K W, et al.Functional and Thermal Properties of Wheat, Barley, and Soy Flours and Their Blends Treated with a Microbial Transglutaminase[J].Journal of Food Science, 2005, 70 (6) :380-386.
[17]	Ionescu A, Aprodu I, Daraba A, et al.The effects of transglutaminase on the functional properties of the myofibrillar protein concentrate obtained from beef heart[J].Meat Science, 2008, 79 (2) :278-284.
[18]	Wang J S, Zhao M M, Yang X Q, et al.Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction[J].Food Hydrocolloids, 2007, 21 (2) :174-179.
[19]	Lorenzen P C.Effects of varying time/temperature-conditions of preheating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients[J].Food Research International, 2007, 40 (6) :700-708.
[20]	Yildirim M, Hettiarachchy N S, Kalapathy U.Properties of Biopolymers from Cross-linking Whey Protein Isolate and Soybean11S Globulin[J].Journal of Food Science, 1996, 61 (6) :1129-1132.