Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis

Karin Buettner1, T. Hertel1, Markus Pietzsch1
1Department of Downstream Processing, Institute of Pharmacy, Faculty of Sciences I, Martin Luther University Halle-Wittenberg, 06099, Halle (Saale), Germany

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Ando H, Adachi M, Umeda K, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M (1989) Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric Biol Chem 53(10):2613–2617

Beninati S, Piacentini M (2004) The transglutaminase family: an overview: minireview article. Amino Acids 26(4):367–372

Cadwell RC, Joyce GF (1992) Randomization of genes by PCR mutagenesis. PCR Methods Appl 2(1):28–33

Cadwell RC, Joyce GF (1994) Mutagenic PCR. PCR Methods Appl 3(6):S136–S140

Chambi H, Grosso C (2006) Edible films produced with gelatin and casein cross-linked with transglutaminase. Food Res Int 39:458–466

de Jong GA, Koppelman SJ (2002) Transglutaminase catalyzed reactions: impact on food applications. J Food Sci 67(8):2798–2806

Folk JE, Cole PW (1966) Transglutaminase: mechanistic features of the active site as determined by kinetic and inhibitor studies. Biochim Biophys Acta 122(2):244–264

Giver L, Gershenson A, Freskgard P-O, Arnold FH (1998) Directed evolution of a thermostable esterase. Proc Natl Acad Sci USA 95(22):12809–12813

Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer. An environment for comparative protein modeling. Electrophoresis 18(15):2714–2723

Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matsui H, Suzuki E (2002) Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J Biol Chem 277(46):44252–44260

Longo MA, Combes D (1999) Thermostability of modified enzymes: a detailed study. J Chem Technol Biotechnol 74(1):25–32

Lorimer IAJ, Pastan I (1995) Random recombination of antibody single chain Fv sequences after fragmentation with DNasel in the presence of Mn2+. Nucleic Acids Res 23(15):3067–3068

Lowman HB, Wells JA (1993) Affinity maturation of human growth hormone by monovalent phage display. J Mol Biol 234(3):564–578

Marx C, Hertel T, Pietzsch M (2007) Soluble expression of a pro-transglutaminase from Streptomyces mobaraensis in Escherichia coli. Enzyme Microb Technol 40:1543–1550

Marx CK, Hertel TC, Pietzsch M (2008a) Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in E. coli and characterization of the active enzyme. Enzyme Microb Technol 42:568–575

Marx CK, Hertel TC, Pietzsch M (2008b) Random mutagenesis of a recombinant microbial transglutaminase for the generation of thermostable and heat sensitive variants. J Biotechnol 136:156–162

Maullu C, Raimondo D, Caboi F, Giorgetti A, Sergi M, Valentini M, Tonon G, Tramontano A (2009) Site-directed enzymatic PEGylation of the human granulocyte colony-stimulating factor. FEBS J 276(22):6741–6750

McLachlan MJ, Johannes TW, Zhao H (2008) Further improvement of phosphite dehydrogenase thermostability by saturation mutagenesis. Biotechnol Bioeng 99(2):268–274

Miyazaki K, Arnold FH (1999) Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J Mol Evol 49(6):716–720

O’Fagain C (2003) Enzyme stabilization—recent experimental progress. Enzyme Microb Technol 33(2–3):137–149

Oh J-H, Wang B, Field PD, Aglan HA (2004) Characteristics of edible films made from dairy proteins and zein hydrolysate cross-linked with transglutaminase. Int J Food Sci Technol 39(3):287–294

Pace CN, Schmid FX (1997) How to determine the molar absorption coefficient of a protein. Protein structure: a practical approach. IRL Press, Oxford

Park Y-M, Phi QT, Song B-H, Ghim S-Y (2009) Thermostability of chimeric cytidine deaminase variants produced by DNA shuffling. J Microbiol Biotechnol 19(12):1536–1541

Patzsch K, Riedel K, Pietzsch M (2010) Parameter optimization for protein film production using microbial transglutaminase. Biomacromolecules 11:896–903

Sato H (2002) Enzymatic procedure for site-specific pegylation of proteins. Adv Drug Deliv Rev 54(4):487–504

Schrodinger LLC (2010) The PyMOL Molecular Graphics System, Version 1.3r1

Shimba N, Shinohara M, Yokoyama K, Kashiwagi T, Ishikawa K, Ejima D, Suzuki E (2002) Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Lett 517(1–3):175–179

Sommer C, Hertel TC, Schmelzer CEH, Pietzsch M (2011a) Investigations on the activation of recombinant microbial pro-transglutaminase: in contrast to Proteinase K, Dispase removes the Histidine-tag. Amino Acids. doi: 10.1007/s00726-011-1016-x (this issue)

Sommer C, Volk N, Pietzsch M (2011b) Model based optimization of the fed-batch production of a highly active transglutaminase variant in E. coli. Protein Expr Purif 77:9–19

Stemmer WPC (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature (London) 370(6488):389–391

Stratagene (2007) QuikChange site-directed Mutagenesis Kit. Manufacturer’s Manual

Yokoyama K, Utsumi H, Nakamura T, Ogaya D, Shimba N, Suzuki E, Taguchi S (2010) Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl Microbiol Biotechnol 87(6):2087–2096

Yuan L, Kurek I, English J, Keenan R (2005) Laboratory-directed protein evolution. Microbiol Mol Biol Rev 69(3):373–392

Zheng L, Baumann U, Reymond JL (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res 32(14):e115/111–e115/115