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重组解脂耶氏酵母生产谷氨酰胺转胺酶酶原的发酵优化 被引量:1

Fermentation optimization of pro-transglutaminase produced by a recombinant Yarrowia lipolytica strain
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摘要 谷氨酰胺转胺酶(EC2.3.2.13,TGase)是一种重要的食品酶,广泛应用于食品组分的质构、起泡性及乳化性等功能性质的改善。以一株分泌谷氨酰胺转胺酶酶原(pro-TGase)的重组解脂耶氏酵母Yarrowia lipolytica BBETG为研究对象,结合单因素实验与正交实验对其发酵培养基进行优化,以期实现pro-TGase的高产。结果表明,较优的发酵培养基配方为:甘油15 g/L、酵母膏20 g/L、氯化铵2.64 g/L、KH2PO4 0.32 g/L、无水MgSO4 0.25 g/L、VB13.34×10-4 g/L,初始pH值8.0。在该培养基中,重组菌于28℃发酵120 h,获得的pro-TGase经体外活化,酶活达8.47 U/mL,较初始发酵培养基产量提高393%。 Transglutaminase (EC 2.3.2.13, TGase) is an important enzyme that has been widely used to improve the functional properties of food ingredients, such as texture, foamability and emulsibility. In this study, the fermentation medium of a recombinant Yarrowia lipolytica strain BBETG that secreted pro- transglutaminase (pro-TGase) was optimized through single-factor and orthogonal tests. The optimal fermentation medium was consisted of 15 g/L glycerol, 20 g/L yeast extract, 2.64 g/L NH4Cl, 0.32 g/L KH2PO4, 0.25 g/L MgSO4, 3.34×10-4 g/L VB1 at pH 8.0. When fermented in the optimized medium at 28 ℃ for 120 h, the yield of pro-TGase corresponded to 8.47 U/mL of TGase, which was 393% higher than that at initial conditions.
出处 《食品科技》 CAS 北大核心 2014年第4期5-9,共5页 Food Science and Technology
基金 国家自然科学基金项目(31171639) "十二五"农村领域国家科技计划课题(2011AA1009000) 国家863项目(2011AA100905)
关键词 重组解脂耶氏酵母 谷氨酰胺转胺酶 培养基优化 recombinant Yarrowia lipolytica pro-transglutaminase fermentation optimization
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  • 1Olempska-Beer Z S, et al. Food-processing enzymes from recombinant microorganisms-a review[J]. Regulatory toxicology and Pharmacology,2006,45(2):144-158.
  • 2Zbang D, Y Zhn, J Chen. Microbial transglutaminase production: understanding the mechanism[J]. Biotechnology and Genetic Engineering Reviews,2009,26(1):205-222.
  • 3Shleikin A G, N P Danilov. Evolutionary-biological peculiarities of transglutaminase. Structure, physiological functions, application[J]. Journal of Evolutionary Biochemistry and Physiology,2011,47(1):1-14.
  • 4Marx C K, T C Hertel, M Pietzsch. Purification and activation of a recombinant histidine-tagged pro- transglutaminase after soluble expression in Escherichia coli and partial characterization of the active enzyme[J]. Enzyme and Microbial Technology,2008,42(7):568-575.
  • 5Yokoyama K, N Nio, Y Kikuchi. Properties and applications of microbial transglutaminase[J]. Applied Microbiology and Bioteehnology,2004,64(4):447-454.
  • 6Aeschlimann D, M Paulsson. Transglutaminases-Protein Cross-Linking Enzymes in Tissues and Body-Fluids[J]. Thrombosis and Haemostasis, 1994,71 (4):402-415.
  • 7Serafini-Fracassini D, S Delduca, S Beninati. Plant Transglutaminases[J]. Phytochemistry, 1995,40(2):355-365.
  • 8Ando H, et al. Purification and characteristics of a novel transglutaminase derived from microorganisms[J]. Agricultural and Biological Chemistry,1989,53(10):2613- 2617.
  • 9Lin YS, et al. Cloning and expression of the transglutaminase gene from Streptoverticillium ladakanum in Streptomyces lividans[J]. Process Biochemistry,2004,39(5):591-598.
  • 10Cui L, et al. Purification and characterization of trans- glutaminase from a newly isolated Streptomyces hwrosconicus[J1. Food chemistry,2007,105(2):612-618.

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