The effect of transglutaminase (TGase) on the thermostability of goat milk after heat pretreatment was studied. The results showed that the heat coagulation time (HCT) of goat milk significantly increased by increasing temperature and time (P<0.05). Pretreatment of goat milk at 60-70°C for 60 min or at 80-90°C for 30 min could completely inactivate the natural TGase inhibitor in the goat milk and could denature the milk protein. Additionally, the higher temperature the more milk protein was denatured, which was benefit for the cross-linking of milk protein by TGase. The existence of natural TGase inhibitor in the goat milk was further confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Heat pretreatment could increase the cross-linking degree of κ-casein mediated by TGase, which also prevented the dissociation of κ-casein from casein micelles and further improved the thermostability of the goat milk.
CHEN Si
,
ZHANG Fuxin
,
WANG Bini
,
SHAO Yuyu
,
CAO binyun
. Effect of heat pretreatment on thermostability of goat milk catalyzed by transglutaminase[J]. Food and Fermentation Industries, 2019
, 45(2)
: 25
-30
.
DOI: 10.13995/j.cnki.11-1802/ts.018060
[1] RAYNAL-LJUTOVAC K, PARK Y W, GAUCHERON F, et al. Heat stability and enzymatic modifications of goat and sheep milk[J] . Small Ruminant Research, 2007, 68(1): 207-220.
[2] WANG C, ZHU Y, WANG J. Comparative study on the heat stability of goat milk and cow milk[J] . Indian Journal of Animal Research, 2015,50(4):610-613.
[3] 乔星,张富新,乌素,等. 羊奶热稳定因素的研究[J] . 农产品加工(学刊), 2012(1): 46-48.
[4] KASHIWAGI T, YOKOYAMA K, ISHIKAWA K, et al. Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense[J] . Journal of Biological Chemistry, 2002, 277(46): 44252-44260.
[5] 司晶星,张瑾,翟付群. 谷氨酰胺转氨酶生产及研究进展[J] . 商业文化(下半月), 2009(6): 229.
[6] 寇明钰,赵国华,阚健全. 谷氨酰胺转胺酶及其在食品工业中的作用[J] . 中国食品添加剂, 2004(5): 81-84, 88.
[7] O'SULLIVAN M M, LORENZEN P C, O’CONNELL J E, et al. Short communication: influence of transglutaminase on the heat stability of milk[J] . Journal of Dairy Science, 2001, 84(6): 1331-1334.
[8] ROMEIH E, WALKER G. Recent advances on microbial transglutaminase and dairy application[J] . Trends in Food Science & Technology, 2017, 62:133-140.
[9] RODRIGUEZNOGALES J M. Enhancement of transglutaminase-induced protein cross-linking by preheat treatment of cows' milk: A statistical approach[J] . International Dairy Journal, 2006, 16(1): 26-32.
[10] DE JONG G A H, WIJNGAARDS G, KOPPELMAN S J. Transglutaminase inhibitor from milk[J] . Journal of Food Science, 2003, 68(3): 820-825.
[11] BÖNISCH M P, TOLKACH A, KULOZIK U. Inactivation of an indigenous transglutaminase inhibitor in milk serum by means of UHT-treatment and membrane separation techniques[J] . International Dairy Journal, 2006, 16(6): 669-678.
[12] O’CONNELL J E, FOX P F. Heat-induced coagulation of milk[M] . Boston, MA: Springer US, 2003: 879-945.
[13] GROSSOWICZ N, WAINFAN E, BOREK E, et al. The enzymatic formation of hydroxamic acids from glutamine and asparagine[J] . Journal of Biological Chemistry, 1950, 187(1): 111-25.
[14] ANEMA S G, STANLEY D J. Heat-induced, pH-dependent behaviour of protein in caprine milk[J] . International Dairy Journal, 1998, 8(10): 917-923.
[15] DE JONG G A H, WIJNGAARDS G, KOPPELMAN AND S J. Transglutaminase inhibitor from milk[J] . Food Chemistry and Toxicology, 2003,68(3):820-825.
[16] 赵丽丽. 羊乳热稳定性及凝胶特性的研究[D] . 北京:中国农业科学院, 2014.
[17] LAEMMLI U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J] . Nature, 1970, 227(5259): 680-685.
[18] O'SULLIVAN M M, KELLY A L, FOX P F. Effect of transglutaminase on the heat stability of milk: A possible mechanism[J] . Journal of Dairy Science, 2002, 85(1): 1-7.
[19] AALTONEN T, HUUMONEN I, MYLLÄRINEN P. Controlled transglutaminase treatment in Edam cheese-making[J] . International Dairy Journal, 2014, 38(2): 179-182.
[20] IKURA K, MINAMI K, OTOMO C, et al. High molecular weight transglutaminase inhibitor produced by a microorganism (Streptomyces lavendulae Y-200)[J] . Bioscience Biotechnology & Biochemistry, 2000, 64(1): 116-124.
[21] RAJAKARI K. Structure modification of sour milk products by transglutaminase[D] . Helsinki: Aalto University, 2015.
[22] MP B N, M H, K W, et al. Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties[J] . International Dairy Journal, 2007, 17(11): 1360-1371.
[23] TATERKA H, CASTILLO M. The effect of whey protein denaturation on light backscatter and particle size of the casein micelle as a function of pH and heat-treatment temperature[J] . International Dairy Journal, 2015, 48(3): 53-59.
[24] WALSTRA P. On the stability of casein micelles 1[J] . Journal of Dairy Science, 1990, 73(8): 1965-1979.
[25] RODRIGUEZ-NOGALES J M. Effect of preheat treatment on the transglutaminase-catalyzed cross-linking of goat milk proteins[J] . Process Biochemistry, 2006, 41(2): 430-437.
[26] SHARMA R, LORENZEN P C, QVIST K B. Influence of transglutaminase treatment of skim milk on the formation of epsilon-(gamma-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking[J] . International Dairy Journal, 2001, 11(10): 785-793.