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[1] Bornscheuer U T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev, 2002, 26(1):73-81.
[2] Manco G, Adinolfi E, Pisani F M, et al. Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormonesensitive lipase subfamily. Biochem J, 1998, 332:203-212.
[3] Mandrich L, Manco G, Rossi M, et al. Alicyclobacillus acidocaldarius thermophilic esterase EST2's activity in milk and cheese models. Appl Environ Microbiol, 2006, 72(5):3191-3197.
[4] Ferdinando F, Luigia M, Giovanni PC, et al. Thermostable esterase 2 from Alicyclobacillus acidocaldarius as biosensor for the detection of organophosphate pesticides. Anal Chem, 2011, 83:1530-1536.
[5] De Simone G, Manco G, Galdiero S, et al. Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius. Acta Cryst, 1999, 55, 1348-1349.
[6] Manco G, Mandrich L, Rossi M. Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature. J Biol Chem, 2001, 276:37482-37490.
[7] Pezzullo M, Del Vecchio P, Mandrich L, et al. Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2. Protein Eng Des Sel, 2013, 26(1):47-58.
[8] Foglia F, Mandrich L, Pezzullo M, et al. Role of the N-terminal region for the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius. Biophys Chem, 2007, 127:113-122.
[9] Mandrich L, Merone L, Pezzullo M, et al. Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family, J Mol Biol,2005, 345(3):501-512.
[10] Schiraldi C, Acone M, Giuliano M, et al. Innovative fermentation strategies for the production of extremophilic enzymes. Extremophiles, 2001, 5(3):193-198.
[11] Demain A L, Vaishnav P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv, 2009, 27(3):297-306.
[12] McHunu N P, Singh S, Permaul K. Expression of an alkalo-tolerant fungal xylanase enhanced by directed evolution in Pichia pastoris and Escherichia coli. J Biotechnol, 2009, 141(1-2): 26-30.
[13] Sriyapai T, Somyoonsap P, Matsui K, et al. Cloning of a thermostable xylanase from Actinomadura sp. S14 and its expression in Escherichia coli and Pichia pastoris. J Biosci Bioeng, 2011, 111(5):528-536.
[14] Zhou K, He H X, Wang X W, et al. Cloning, expression and bioactivity of hemagglutinin binding domain protein of avian influenza virus in the yeast Pichia pastoris and E.coli. Progress on Post-genome Technologies, Proceedings of the 6'th International Forum of Post-genome Technologies (IFPT'6), Beijing, China, 2009.
[15] Kramer W, Elmecker G, Weik R, et al. Kinetic studies for the optimization of recombinant protein formation. Ann NY Acad Sci, 1996, 782: 323 -333.
[16] Tripathi N K. High yield production of heterologous proteins with Escherichia coli. De Sci J, 2009, 59:137-146.
[17] Pei X L, Wang Q, Qiu X, et al. The fed-batch production of a thermophilic 2-deoxyribose-5-phosphate aldolase (DERA) in Escherichia coli by exponential feeding strategy control. Appl Biochem Biotechnol, 2010, 162(5):1423-1434.
[18] Pei X L, Wang Q Y, Li C L, et al. Efficient production of a thermophilic 2-deoxyribose-5-phosphate aldolase in glucose-limited fed-batch cultivations of Escherichia coli by continuous lactose induction strategy. Appl Biochem Biotechnol, 2011, 165(2):416-425.
[19] Ren X, Yu D, Han S, et al. Optimization of recombinant hyperthermophilic esterase production from agricultural waste using response surface methodology. Bioresour Technol, 2006, 97(18):2345-2349.
[20] Ren X, Yu D, Yu L, et al. A new study of cell disruption to release recombinant thermostable enzyme from Escherichia coli by thermolysis. J Biotechnol, 2007, 129(4):668-673.
[21] Daly R, Hearn M T. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit, 2005, 18(2):119-138.
[22] Liu L, Yang H, Shin H D, et al. How to achieve high-level expression of microbial enzymes: strategies and perspectives. Bioengineered, 2013, 4(4):212-223.
[23] Menéndez C, Martínez D, Trujillo L E, et al. Constitutive high-level expression of a codon-optimized β-fructosidase gene from the hyperthermophile Thermotoga maritima in Pichia pastoris. Appl Microbiol Biotechnol, 2013, 97(3):1201-1212.
[24] Yan Q, Hua C, Yang S, Li Y, et al. High level expression of extracellular secretion of a β-glucosidase gene(PtBglu3) from Paecilomyces thermophila in Pichia pastoris. Protein Expr Purif, 2012, 84(1):64-72.
[25] Fan G, Katrolia P, Jia H, et al. High-level expression of a xylanase gene from the thermophilic fungus Paecilomyces thermophila in Pichia pastoris. Biotechnol Lett, 2012, 34(11):2043-2048.
[26] Jia H Y, Fan G S, Yan Q J, et al. High-level expression of a hyperthermostable Thermotoga maritima xylanase in Pichia pastoris by codon optimization. J Mol Catal B: Enzym, 2012, 78: 72-77.
[27] Xie Y, An J, Yang G, et al. Enhanced enzyme kinetic stability by increasing rigidity within the active site. J Biol Chem, 2014, 289(11):7994-8006.
[28] Yang G, Bai A, Gao L, et al. Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability. Biochim Biophys Acta, 2009, 1794(1): 94-102.
[29] Zheng J, Zhao W, Guo N, et al. Development of an industrial medium and a novel fed-batch strategy for high-level expression of recombinant β-mananase by Pichia pastoris. Bioresour Technol, 2012, 118: 257-264.
[30] Damasceno L M, Pla I, Chang H J, et al. An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris. Protein Expr Purif, 2004, 37(1): 18-26.
[31] Huang H, Yang P, Luo H, et al. High-level expression of a truncated 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes in Pichia pastoris by optimization of codons and fermentation. Appl Microbiol Biotechnol. 2008, 78(1): 95-103.
[32] Chen C, Wu PH, Huang C T, et al. A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase. Enzyme Microb Technol, 2004, 35: 315–320.
[33] Xie J, Zhou Q, Du P, et al. Use of different carbon sources in cultivation of recombinant Pichia pastoris for angiostatin production. Enzyme Microb Technol, 2005, 36: 210-216.
[34] Liu B, Lei Y T, Zhang J, et al. Expression, purification and characterization of recombinant human gelatin in Pichia pastoris. Advanced Materials Research, 2011, 236: 2905-2912.
[35] Riesenberg D, Guthke R. High-cell-density cultivation of microorganisms. Appl Microbiol Biotechnol, 1999, 51(4):422-430.
[36] Soares C R, Gomide F I, Ueda E K, et al. Periplasmic expression of human growth hormone via plasmid vectors containing the lambdaPL promoter: use of HPLC for product quantification. Protein Eng, 2003, 16(12):1131-1138.
[37] Ohta K, Shibui T, Morimoto Y, et al. High level production of human proapo A-I by fed-batch culture of recombinant Escherichia coli. Journal of Fermen and Bioeng, 1993, 75(2): 155-157.
[38] Ma X, Su E, Zhu Y, et al. High-level expression of glutaryl-7-aminocephalosporanic acidacylase from Pseudomonas diminuta NK703 in Escherichia coli bycombined optimization strategies. J Biotechnol, 2013, 168(4):607-615.
[39] Baheri H R, Roesler W J, Hill G A, et al. Modeling of recombinant bacteria fermentation for enhanced productivity. Biotechnol Tech, 1997, 11(1): 47-50.
[40] 丁兰宝,牛丹丹,石贵阳,等. 重组大肠杆菌表达古菌基因的发酵条件优化.食品工业科技,2008, 29:97-102. Ding L B, Niu D D, Shi G Y, et al. Optimization of fermentation conditions of recombinant E.coli for production of archaeal thermostable acidic α-amylase. Science and Technology of Food Industry, 2008, 29:97-102.
[41] Sitney K C, Mann M B, Stearns G W, et al. Use of a modified tryptophanase promoter to direct high-level expression of foreign proteins in E. coli. Ann N Y Acad Sci, 1996, 782:297-310.
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