|
[1] 贾建波, 李相前, 胡敏. 脂肪酶基因在枯草芽孢杆菌中的表达及表达产物性质的研究. 中国生物工程杂志,2008, 28(1): 25-29. Jia J B, Li X Q, Hu M. Expression and characterization of a lipase in Bacillus subtilis. China Biotechnology,2008, 28(1): 25-29.
[2] Yang M M, Zhang W W, Zhang X F, et al. Construction and characterization of a novel maltose inducible expression vector in Bacillus subtilis. Biotechnol Lett, 2006, 28(21): 1713-1718.
[3] 彭清忠, 张惟材, 朱厚础. 枯草杆菌表达系统的研究进展.生物技术通讯, 2001, 12(3): 220-225. Peng Q Z, Zhang W C, Zhu H C. Progress in the expressing system of Bacillus subtilis. Letters in Biotechnology, 2001, 12(3): 220-225.
[4] Westers H, Braun PG, Westers L, et al. Genes involved in SkfA killing factor production protect a Bacillus subtilis lipase against proteolysis. Appl Environ Microbiol, 2005, 71(4):1899-1908.
[5] 胡艳华, 李敏, 石爱琴. 胞外脂肪酶在枯草芽孢杆菌中的表达与其性质. 浙江理工大学学报, 2009, 26(5):757-763. Hu Y H, Li M, Shi A Q. Expression and analysis of an extracellular lipase in Bacillus subtilis. Journal of Zhejiang Sci-Tech University 2009, 26(5):757-763.
[6] 何敏, 脂肪酶产生菌的筛选及其酶基因在枯草芽孢杆菌中的整合表达. 四川:四川农业大学, 动物医学院,2011. He M. Screening of Lipase Producing Strains and the Integrative Expression of Lipase Genes in Bacillus subtilis. Sichuan: Sichuan Agricultural University, College of Veterinary Medicine,2011.
[7] Olusesan A T, Azura L K, Abubakar F, et al. Enhancement of thermostable lipase production by a genotypically identified extremophilic Bacillus subtilis NS 8 in a continuous bioreactor. J Mol Microbiol Biotechnol. 2011, 20(2): 105-115.
[8] 沈兴中. 枯草芽孢杆菌lipA基因启动子的修饰及其表达. 天津:天津大学, 化工学院,2008. Shen X Z. Modification and Expression of lipA Promoter in Bacillus subtilis. Tianjin: Tianjin University, College of Chemical Engineering,2008.
[9] Lu Y P, Lin Q, Wang J, et al. Overexpression and characterization in Bacillus subtilis of a positionally nonspecific lipase from Proteus vulgaris. J Ind Microbiol Biotechnol, 2010, 37(9): 919-925.
[10] 夏雨, 成玉梁, 李达倩,等. 枯草芽孢杆菌分泌载体构建及其对脂肪酶A的分泌表达. 安徽农业科学, 2011, 39(30): 18435-18437. Xia Y, Cheng Y L, Li D Q, et al. Construction of secretory expression vectors for Bacillus subtilis and secretion of lipase A, Journal of Anhui Agri. Sci, 2011, 39(30): 18435-18437.
[11] 崔静, 王光强, 陈海琴,等. 利用非经典分泌蛋白质实现脂肪酶 A 的分泌表达. 微生物学报, 2015, 55(2): 198-204. Cui J, Wang G Q, Chen H Q, et al. Effect of non-classical secreted proteins on LipaseA secretion. Acta Microbiologica Sinica, 2015, 55(2): 198-204.
[12] Sambrook J, Russell D W. Molecular Cloning: A Laboratory Manual. 3rd ed. New York: Cold Spring Harbor Laboratory Press, 2001.
[13] Spizizen J. Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc Natl Acad Sci, 1958 44(10):1072-1078.
[14] 李牧. 嗜麦芽糖寡养单胞菌脂肪酶的筛选、异源表达及在催化制备l-薄荷醇中的应用. 杭州: 浙江大学, 化学工程与生物工程学院,2012. Li M. Screening and Heterologous Expression of Stenotrophomonas maltophilia Lipase, and Its Application in Enzymatic Preparation of l-menthol. Hangzhou: Zhejiang University, College of Chemical and Biological Engineering,2012.
[15] Brockmeier U, Caspers M, Freud R, et al. Systematic screening of all signal peptides from Bacillus subtilis: A powerful strategy in optimizing heterologous protein secretion in Gram-positive Bacteria. J Mol Biol, 2006, 362(3): 393-402.
[16] Tjalsma H, Bolhuis H, Jongbloed J D, et al. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol Mol Biol Rev, 2000, 64(3): 515-547.
[17] Robinson C, Bolhuis A. Protein targeting by the twin-arginine translocation pathway. Nature Reviews Molecular Cell Biology, 2001, 2(5): 350-356.
[18] Sarvas, M, Harwood C R, Bron S, et al. Post-translocational folding of secretory proteins in Gram-positive bacteria. Biochimica et Biophysica Acta, 2004, 1694(1-3): 311-327.
[19] Jung J, Yu K O, Ramzi A B, et al. Improvement of surfactin production in Bacillus subtilis using synthetic wastewater by overexpression of specific extracellular signaling peptides, comX and phrC. Biotechnology and Bioengineering, 2012, 109(9): 2349-2356.
[20] Luan C, Zhang H W, Song D G, et al. Expressing antimicrobial peptide cathelicidin-BF in Bacillus subtilis using SUMO technology. Appl Microbiol Biotechnol, 2014, 98(8): 3651-3658.
[21] Phan T T P, Schumann W. Development of a glycine-inducible expression system for Bacillus subtilis. Journal of Biotechnology, 2007, 128(3): 486-499.
[22] Wu J P, Li M, Zhou Y, et al. Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability. Biotechnol Lett, 2015, 37(2): 403-407.
[23] Pop O I, Westermann M, Volkmer-Engert R, et al. Sequence- specific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis. The Journal of Biological Chemistry, 2003, 278(40): 38428-38436.
[24] Klein M J, Grage S L, Muhle-Goll C, et al. Structure analysis of the membrane-bound PhoD signal peptide of the Tat translocase shows an N-terminal amphiphilic helix. Biochimica et Biophysica Acta, 2012, 1818(12): 3025-3031.
[25] Wu B, He M X, Feng H, et al. Construction of a novel secretion expression system guided by native signal peptide of PhoD in Zymomonas mobilis. Bioscience Biotechnology and Biochemistry, 2014, 78(4): 708-713.
|
