title: [Progress in expression and molecular modification of microbial transglutaminase].
abstract: Microbial transglutaminase, which could catalyze the cross-linking of many proteins or non-protein materials, has been widely used in food, pharmaceutical and textile industry. To enhance the yield of the enzyme and establish corresponding platform for molecular modification, the researchers of Japanese Ajinomoto began to construct the recombinant strain producing transglutaminase in the 1990s. So far, the enzyme has been successfully expressed in different expression systems. Some of the recombinant strains are more productive than wild strains. Recently, progress has been made in the molecular modification of microbial transglutaminase, and the activity, thermo-stability and specificity of the enzyme are improved. This review briefly summarized and analyzed the strategies involved in these studies, and noted its trends.
authors.affiliation: Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China.
authors.forename: Song
authors.initials: S
authors.lastname: Liu
authors.forename: Dongxu
authors.initials: D
authors.lastname: Zhang
authors.forename: Guocheng
authors.initials: G
authors.lastname: Du
authors.forename: Jian
authors.initials: J
authors.lastname: Chen
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics; D002384:Catalysis; D004795:Enzyme Stability; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D011503:Transglutaminases / Q000096:biosynthesis* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D050505:Mutant Proteins; D011503:Transglutaminases