1,308
Views
22
CrossRef citations to date
0
Altmetric
Biochemistry & Molecular Biology (Note)

Improvement of the activity and thermostability of microbial transglutaminase by multiple-site mutagenesis

, , , , , , , , & show all
Pages 106-109 | Received 27 Jul 2017, Accepted 04 Nov 2017, Published online: 04 Dec 2017

References

  • Ohtsuka T, Sawa A, Kawabata R, et al. Substrate specificities of microbial transglutaminase for primary amines. J Agric Food Chem. 2000;48(12):6230–6233.10.1021/jf000302k
  • Yokoyama K, Nio N, Kikuchi Y. Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol. 2004;64(4):447–454.10.1007/s00253-003-1539-5
  • Clare DA, Gharst G, Maleki SJ, et al. Effects of transglutaminase catalysis on the functional and immunoglobulin binding properties of peanut flour dispersions containing casein. J Agric Food Chem. 2008;56(22):10913–10921.10.1021/jf801641d
  • Li C, Xiong YL, Chen J. Oxidation-induced unfolding facilitates myosin cross-linking in myofibrillar protein by microbial transglutaminase. J Agric Food Chem. 2012;60(32):8020–8027.10.1021/jf302150 h
  • Aloisi I, Cai G, Serafini-Fracassini D, et al. Transglutaminase as polyamine mediator in plant growth and differentiation. Amino Acids. 2016;48(10):2467–2478.10.1007/s00726-016-2235-y
  • Liu S, Zhang D, Wang M, et al. The order of expression is a key factor in the production of active transglutaminase in Escherichia coli by co-expression with its pro-peptide. Microb Cell Fact. 2011; 10:112. DOI:10.1186/1475-2859-10-112
  • Dickneite G, Herwald H, Korte W, et al. Coagulation factor XIII: a multifunctional transglutaminase with clinical potential in a range of conditions. Thromb Haemost. 2015;113(4):686–697.10.1160/TH14-07-0625
  • Pasternack R, Dorsch S, Otterbach JT, et al. Bacterial pro-transglutaminase from Streptoverticillium mobaraense – purification, characterisation and sequence of the zymogen. Eur J Biochem. 1998;257(3):570–576.10.1046/j.1432-1327.1998.2570570.x
  • Chen K, Liu S, Wang G, et al. Enhancement of Streptomyces transglutaminase activity and pro-peptide cleavage efficiency by introducing linker peptide in the C-terminus of the pro-peptide. J Ind Microbiol Biotechnol. 2013;40(3–4):317–325.10.1007/s10295-012-1221-y
  • Chen K, Liu S, Zhang D, et al. Altered secretary efficiency of Streptomyces hygroscopicus transglutaminase in Escherichia coli by the pro-peptide modification. Process Biochem. 2013;48(5):782–787.10.1016/j.procbio.2013.04.001
  • Gaspar AL, de Goes-Favoni SP. Action of microbial transglutaminase (MTGase) in the modification of food proteins: a review. Food Chem. 2015;171:315–322.10.1016/j.foodchem.2014.09.019
  • Kieliszek M, Misiewicz A. Microbial transglutaminase and its application in the food industry. Folia Microbiol (Praha). 2014;59(3):241–250.10.1007/s12223-013-0287-x
  • Rachel NM, Pelletier JN. Biotechnological applications of transglutaminases. Biomolecules. 2013;3(4):870–888.10.3390/biom3040870
  • Zhu Y, Tramper J. Novel applications for microbial transglutaminase beyond food processing. Trends Biotechnol. 2008;26(10):559–565.10.1016/j.tibtech.2008.06.006
  • Buettner K, Hertel TC, Pietzsch M. Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis. Amino Acids. 2012;42(2–3):987–996.10.1007/s00726-011-1015-y
  • Yokoyama K, Utsumi H, Nakamura T, et al. Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl Microbiol Biotechnol. 2010;87(6):2087–2096.10.1007/s00253-010-2656-6
  • Marx CK, Hertel TC, Pietzsch M. Random mutagenesis of a recombinant microbial transglutaminase for the generation of thermostable and heat-sensitive variants. J Biotechnol. 2008;136(3–4):156–162.10.1016/j.jbiotec.2008.06.005
  • Yang HL, Pan L, Lin Y. Purification and on-column activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli. Biosci Biotechnol Biochem. 2009;73(11):2531–2534.10.1271/bbb.90422
  • Grossowicz N, Wainfan E, Borek E, et al. The enzymatic formation of hydroxamic acids from glutamine and asparagine. J Biol Chem. 1950;187(1):111–125.
  • Kashiwagi T, Yokoyama K, Ishikawa K, et al. Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J Biol Chem. 2002;277(46):44252–44260.10.1074/jbc.M203933200
  • Ando H, Adachi M, Umeda K, et al. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric Biol Chem. 1989;53(10):2613–2617.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.