Recent advances in high-level heterologous expression of microbial enzymes

doi:10.7506/spkx1002-6630-201309070

Abstract

Abstract: Enzyme is a kind of biological catalyst with high specificity and has been widely used in chemical industry, agricultural industry, biopharmaceutical industry, food industry, textile industry, feed industry and other industries. The commonly used industrial enzyme expression hosts include Escherichia coli, Bacillus, filamentous fungi, yeast, and lactic acid bacteria. Different expression hosts have different characteristics. For example, the bacterium hosts can quickly and easily over-express recombinant enzymes, but the bacterium systems cannot express very large eukaryotic proteins because of proteins requiring post-translational modifications. In recent years, the great progresses have been made in the high-level expression of industrial enzymes in different hosts. In this work, we systematically summarize the recent advances in the heterologous expression of industrial enzymes, and the development trends of heterologous expression of industrial enzymes are also prospected.

YANG Hai-quan，LIU Long，LI Jiang-hua，DU Guo-cheng，CHEN Jian. Recent advances in high-level heterologous expression of microbial enzymes[J]. FOOD SCIENCE, 2013, 34(9): 351-357.

References

参考文献（References）：
[1] Sanchez S, Demain A. Special issue on the production of recombinant proteins [J]. Biotechnology Advances, 2012, 30(5):1100-1101.
[2] Ward OP. Production of recombinant proteins by filamentous fungi [J]. Biotechnology Advance, 2012, 30(5):1119-1139.
[3] E G-F. Lactic acid bacteria: a promising alternative for recombinant protein production [J]. Microbial Cell Factories, 2012, 11:157.
[4] Yang HQ, Liu L, Li JH, et al. Heterologous expression, biochemical characterization, and overproduction of alkaline alpha-amylase from Bacillus alcalophilus in Bacillus subtilis [J]. Microbial Cell Factories, 2011, 10:77.
[5] Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems [J]. Applied Microbiology and Biotechnology, 2006, 72(2):211-222.
[6] kChou CP. Engineering cell physiology to enhance recombinant protein production in Escherichia coli [J]. Applied Microbiology and Biotechnology, 2007, 76(3):521-532.
[7] Celik E, Calik P. Production of recombinant proteins by yeast cells [J]. Biotechnology Advance, 2012, 30(5):1108-1118.
[8] Burgess-Brown NA, Sharma S, Sobott F, et al. Codon optimization can improve expression of human genes in Escherichia coli: A multi-gene study [J]. Protein Expression and Purification, 2008, 59(1):94-102.
[9] Yang HQ, Liu L, Shin H, et al. Comparative analysis of heterologous expression, biochemical characterization optimal production of an alkaline α‐amylase from alkaliphilic Alkalimonas amylolytica in Escherichia coli and Pichia pastoris [J]. Biotechnology Progress, 2012, 29(5):39-47.
[10] Alfasi S, Sevastsyanovich Y, Zaffaroni L, et al. Use of GFP fusions for the isolation of Escherichia coli strains for improved production of different target recombinant proteins [J]. Journal of Biotechnology, 2011, 156(1):11-21.
[11] Lian JZ, Ding SH, Cai J, et al. Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization [J]. Applied Microbiology and Biotechnology, 2009, 82(3):463-470.
[12] Lee C-D, Sun H-C, Hu S-M, et al. An improved SUMO fusion protein system for effective production of native proteins [J]. Protein Science, 2008, 17(7):1241-1248.
[13] Tsunoda Y, Sakai N, Kikuchi K, et al. Improving expression and solubility of rice proteins produced as fusion proteins in Escherichia coli [J]. Protein Expression and Purification, 2005, 42(2):268-277.
[14] Bartual SG, Garcia-Doval C, Alonso J, et al. Two-chaperone assisted soluble expression and purification of the bacteriophage T4 long tail fibre protein gp37 [J]. Protein Expression and Purification, 2010, 70(1):116-121.
[15] Stephens LL, Shonhai A, Blatch GL. Co-expression of the plasmodium falciparum molecular chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI [J]. Protein Expression and Purification, 2011, 77(2):159-165.
[16] Vitikainen M, Hyyryl?inen HL, Kivim?ki A, et al. Secretion of heterologous proteins in Bacillus subtilis can be improved by engineering cell components affecting post‐translocational protein folding and degradation [J]. Journal of Applied Microbiology, 2005, 99(2):363-375.
[17] Gamer M, Starnmen S, Biedendieck R, et al. Bacillus megaterium - An alternative expression system [J]. Journal of Biotechnology, 2007, 131(2):S220-S220.
[18] Radha S, Gunasekaran P. Sustained expression of keratinase gene under PxylA and PamyL promoters in the recombinant Bacillus megaterium MS941 [J]. Bioresource Technology, 2008, 99(13):5528-5537.
[19] Borgmeier C, Biedendieck R, Hoffmann K, et al. Transcriptome profiling of degU expression reveals unexpected regulatory patterns in Bacillus megaterium and discloses new targets for optimizing expression [J]. Applied Microbiology and Biotechnology, 2011, 92(3):583-596.
[20] Tang YQ, Xiao JM, Chen Y, et al. Secretory expression and characterization of a novel peroxiredoxin for zearalenone detoxification in Saccharomyces cerevisiae [J]. Microbiological Research, 2013, 168(1):6-11.
[21] Voronovsky AY, Ryabova EB, Verba EV, et al. Expression of xylA genes encoding xylose isomerases from Escherichia coli and Streptomyces coelicolor in the methylotrophic yeast Hansenula polymorpha [J]. FEMS Yeast Research, 2005, 5(11):1055-1062.
[22] Zhou XX, Chandarajoti K, Truong Quang P, et al. Expression of heparan sulfate sulfotransferases in Kluyveromyces lactis and preparation of 3'-phosphoadenosine-5'-phosphosulfate [J]. Glycobiology, 2011, 21(6):771-780.
[23] Kumar R, Singh J. Expression and secretion of a prokaryotic protein streptokinase without glycosylation and degradation in Schizosaccharomyces pombe [J]. Yeast, 2004, 21(16):1343-1358.
[24] Liu G-L, Li Y, Zhou H-X, et al. Over-expression of a bacterial chitosanase gene in Yarrowia lipolytica and chitosan hydrolysis by the recombinant chitosanase [J]. Journal of Molecular Catalysis B-Enzymatic, 2012, 83:100-107.
[25] Boeer E, Piontek M, Kunze G. XplorA (R) 2-an optimized transformation/expression system for recombinant protein production in the yeast Arxula adeninivorans [J]. Applied Microbiology and Biotechnology, 2009, 84(3):583-594.
[26] Nishikawa M, Hagishita T, Yurimoto H, et al. Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidinii [J]. FEBS Letters, 2000, 476(3):150-154.
[27] Liu YP, Pan JF, Wei PL, et al. Efficient expression and purification of recombinant alcohol oxidase in Pichia pastoris [J]. Biotechnology and Bioprocess Engineering, 2012, 17(4):693-702.
[28] Jia DX, Li JH, Liu L, et al. High-level expression, purification, and enzymatic characterization of truncated poly (vinyl alcohol) dehydrogenase in methylotrophic yeast Pichia pastoris [J]. Applied Microbiology and Biotechnology, 2012, Doi 10.1007/s00253-012-3986-3.
[29] Sasagawa T, Matsui M, Kobayashi Y, et al. High-throughput recombinant gene expression systems in Pichia pastoris using newly developed plasmid vectors [J]. Plasmid, 2011, 65(1):65-69.
[30] Xie J, Zhou Q, Du P, et al. Use of different carbon sources in cultivation of recombinant Pichia pastoris for angiostatin production [J]. Enzyme and Microbial Technology, 2005, 36(2):210-216.
[31] Wang Y, Wang Z, Du G, et al. Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris according to the ratio of methanol to cell concentration [J]. Bioresource Technology, 2009, 100(3):1343-1349.
[32] Demain AL, Vaishnav P. Production of recombinant proteins by microbes and higher organisms [J]. Biotechnology Advance, 2009, 27(3):297-306.
[33] Lopez-Lopez O, Fucinos P, Pastrana L, et al. Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae [J]. Journal of Biotechnology, 2010, 145(3):226-232.
[34] Mormeneo M, Javier Pastor FI, Zueco J. Efficient expression of a Paenibacillus barcinonensis endoglucanase in Saccharomyces cerevisiae [J]. Journal of Industrial Microbiology & Biotechnology, 2012, 39(1):115-123.
[35] Kanjou N, Nagao A, Ohmiya Y, et al. Yeast mutant with efficient secretion identified by a novel secretory reporter, Cluc [J]. Biochemical and Biophysical Research Communications, 2007, 358(2):429-434.
[36] van Rensburg E, den Haan R, Smith J, et al. The metabolic burden of cellulase expression by recombinant Saccharomyces cerevisiae Y294 in aerobic batch culture [J]. Applied Microbiology and Biotechnology, 2012, 96(1):197-209.
[37] Gidijala L, Bovenberg RAL, Klaassen P, et al. Production of functionally active Penicillium chrysogenum isopenicillin N synthase in the yeast Hansenula polymorpha [J]. BMC Biotechnology, 2008, 8(1):29.
[38] Kottmeier K, Müller C, Huber R, et al. Increased product formation induced by a directed secondary substrate limitation in a batch Hansenula polymorpha culture [J]. Applied Microbiology and Biotechnology, 2010, 86(1):93-101.
[39] Yang C-H, Huang Y-C, Chen C-Y, et al. Heterologous expression of Thermobifida fusca thermostable alpha-amylase in Yarrowia lipolytica and its application in boiling stable resistant sago starch preparation [J]. Journal of Industrial Microbiology & Biotechnology, 2010, 37(9):953-960.
[40] Van Ooyen AJJ, Dekker P, Huang M, et al. Heterologous protein production in the yeast Kluyveromyces lactis [J]. FEMS Yeast Research, 2006, 6(3):381-392.
[41] Rocha SN, Abrah?o-Neto J, Cerdán ME, et al. Heterologous expression of a thermophilic esterase in Kluyveromyces yeasts [J]. Applied Microbiology and Biotechnology, 2011, 89(2):375-385.
[42] Kumari A, Gupta R. Extracellular expression and characterization of thermostable lipases, LIP8, LIP14 and LIP18, from Yarrowia lipolytica [J]. Biotechnology Letters, 2012, 34(9):1733-1739.
[43] B?er E, Breuer FS, Weniger M, et al Large-scale production of tannase using the yeast Arxula adeninivorans [J]. Applied Microbiology and Biotechnology, 2011, 92(1):105-114.
[44] Idiris A, Tohda H, Kumagai H, et al. Engineering of protein secretion in yeast: strategies and impact on protein production [J]. Applied Microbiology and Biotechnology, 2010, 86(2):403-417.
[45] Gauthier T, Wang X, Sifuentes J, et al. Trypacidin, a spore-borne toxin from Aspergillus fumigatus, is cytotoxic to lung cells [J]. Plos One, 2012, 7(2):e29906.
[46] Ramamoorthy V, Shantappa S, Dhingra S, et al. veA-dependent RNA-pol II transcription elongation factor-like protein, RtfA, is associated with secondary metabolism and morphological development in Aspergillus nidulans [J]. Molecular Microbiology, 2012, 85(4):795-814.
[47] Cortes-Espinosa DV, Absalon AE, Sanchez N, et al. Heterologous expression of manganese peroxidase in Aspergillus niger and its effect on phenanthrene removal from soil [J]. Journal of Molecular Microbiology and Biotechnology, 2011, 21(3-4):120-129.
[48] Alriksson B, Rose SH, van Zyl WH, et al. Cellulase production from spent lignocellulose hydrolysates by recombinant Aspergillus niger [J]. Applied and Environmental Microbiology, 2009, 75(8):2366-2374.
[49] van den Berg BA, Reinders MJT, Hulsman M, et al. Exploring sequence characteristics related to high-level production of secreted proteins in Aspergillus niger [J]. Plos One, 2012, 7(10):e45869.
[50] Sharma R, Katoch M, Govindappa N, et al. Evaluation of the catalase promoter for expressing the alkaline xylanase gene (alx) in Aspergillus niger [J]. FEMS Microbiology Letters, 2012, 327(1):33-40.
[51] Uchima CA, Tokuda G, Watanabe H, et al. Heterologous expression and characterization of a glucose-stimulated beta-glucosidase from the termite Neotermes koshunensis in Aspergillus oryzae [J]. Applied Microbiology and Biotechnology, 2011, 89(6):1761-1771.
[52] Hirayama K, Watanabe H, Tokuda G, et al. Purification and characterization of termite endogenous beta-1,4-endoglucanases produced in Aspergillus oryzae [J]. Bioscience Biotechnology and Biochemistry, 2010, 74(8):1680-1686.
[53] Yoon J, Maruyama J-i, Kitamoto K. Disruption of ten protease genes in the filamentous fungus Aspergillus oryzae highly improves production of heterologous proteins [J]. Applied Microbiology and Biotechnology, 2011, 89(3):747-759.
[54] Yoon J, Aishan T, Maruyama J-i, et al. Enhanced production and secretion of heterologous proteins by the Filamentous fungus Aspergillus oryzae via disruption of vacuolar protein sorting receptor gene aovps10 [J]. Applied and Environmental Microbiology, 2010, 76(17):5718-5727.
[55] Zou G, Shi S, Jiang Y, et al. Construction of a cellulase hyper-expression system in Trichoderma reesei by promoter and enzyme engineering [J]. Microbial Cell Factories, 2012, 11:21.
[56] Lv D, Wang W, Wei D. Construction of two vectors for gene expression in Trichoderma reesei [J]. Plasmid, 2012, 67(1):67-71.
[57] Mantyla A, Paloheimo M, Hakola S, et al. Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum: a recombinant thermoxylanase for biobleaching of kraft pulp [J]. Applied Microbiology and Biotechnology, 2007, 76(2):377-386.
[58] Qin L-N, Cai F-R, Dong X-R, et al. Improved production of heterologous lipase in Trichoderma reesei by RNAi mediated gene silencing of an endogenic highly expressed gene [J]. Bioresource Technology, 2012, 109:116-122.
[59] Li JJ, Zhang W, Wang C, et al. Lactococcus lactis expressing food-grade beta-galactosidase alleviates lactose intolerance symptoms in post-weaning Balb/c mice [J]. Applied Microbiology and Biotechnology, 2012, 96(6):1499-1506.
[60] Morello E, Bermudez-Humaran L, Llull D, et al. Lactococcus lactis an efficient cell factory for recombinant protein production and secretion [J]. Journal of Molecular and Microbiology Biotechnology, 2008, 14(1-3):48-58.
[61] Salonen N, Nyyssola A, Salonen K, et al. Bifidobacterium iongum l-arabinose isomerase-overexpression in Lactococcus lactis, purification, and characterization [J]. Applied Biochemistry and Biotechnology, 2012, 168(2):392-405.
[62] Hollmann A, Saviello M, Delfederico L, et al. Tight controlled expression and secretion of Lactobacillus brevis SlpA in Lactococcus lactis [J]. Biotechnology Letters, 2012, 34(7):1275-1281.
[63] Narita J, Ishida S, Okano K, et al. Improvement of protein production in lactic acid bacteria using 5′-untranslated leader sequence of slpA from Lactobacillus acidophilus [J]. Applied Microbiology and Biotechnology, 2006, 73(2):366-373.
[64] Liang X, Zhang L, Zhong J, et al. Secretory expression of a heterologous nattokinase in Lactococcus lactis [J]. Applied Microbiology and Biotechnology, 2007, 75(1):95-101.