A novel approach for improving the yield of <i>Bacillus subtilis</i> transglutaminase in heterologous strains

Liu, Yihan; Song, Ligang; Zhang, Xiqing; Liu, Xiaoguang; Wang, Jianling; Lu, Fuping

doi:10.1007/s10295-014-1468-6

Cited by 31 publications

(38 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…cinnamoneum (Duran et al, 1998), Streptoverticillium mobaraense (Kikuchi et al, 2003), Streptoverticillium ladakanum (Tellez-Luis et al, 2004), Streptomyces netropsis (Yu et al, 2008), and Streptoverticillium hygroscopicus (Aidaroos et al, 2011). It has also been reported to be found in Bacillus subtilis spores (Liu et al, 2014).…”

Section: Introductionmentioning

confidence: 77%

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Fawzya¹,

Zilda²,

Chaniago

et al. 2016

Squalen Bull. Marine Fisheries Postharvest Biotech.

View full text Add to dashboard Cite

Transglutaminase (TGase), an enzyme that catalyzes the formation of inter-and intra-molecular -(l-glutamyl) lysine (GL) crosslinks, plays an important role in surimi-based products production. The development and the diversification of surimi-based products have recently been getting popular in Indonesia. These surimi-based products can be made from various types of fish. These products generally exhibit good gel strength properties, depending on the fish type and the processing method used. Transglutaminase plays an important role in generating such properties. Fish's endogenous TGase reduces quickly after it is caught and is almost completely destroyed by freezing it, applying exogenous TGase may improve fish's gel forming ability. Microbial transglutaminase (MTGase) can potentially be used to increase gel properties. In this research, a total of 228 Streptomyces strains from marine and terrestrial environments were screened and selected based on their ability to produce MTGase. Strain TTA 02 SDS 14 exhibited the highest activity; and therefore, it was selected for further study. The 16S-rRNA gene analysis showed that it shared 99% similarity to S. thioluteus. In order to optimize MTGase activity, enzyme production was carried out using six different formulas media, designated as media A, B, C, D, E, and F. The result shows that the highest MTGase activity was observed in medium B that contains pepton (1.5%), MgSO 4 .7H 2 0 (0.1%), KH 2 PO 4 (0.5%), Na 2 HPO 4 (0.5%), soybean powder (2%), potato starch (2%), and glucose (1.5%). The MTGase activity reached the highest level (1.45 U/ml) after 4 days of incubation

show abstract

Section: Introductionmentioning

confidence: 77%

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Fawzya¹,

Zilda²,

Chaniago

et al. 2016

Squalen Bull. Marine Fisheries Postharvest Biotech.

View full text Add to dashboard Cite

show abstract

“…These are recombinant mTgs that are used extensively by food processing industries, and mTgs remain in the processed food to enter the gastrointestinal tract (Lerner and Matthias, 2015a,e). As mentioned before, Table 1 is the summary of strains, including recombinant E. coli , used by the food industry to produce these enzymes, with the corresponding yields (Kieliszek and Misiewicz, 2014; Liu et al, 2014; Salis et al, 2015). The conclusions that can be drawn from the data presented in these two tables are:…”

Section: Mtgs Are Expressed and Secreted Into The Human Intestinal Lumenmentioning

confidence: 99%

“…Examples of the mean mTg yield by bacteria used in industrial mTg production (Table No 2), (Kieliszek and Misiewicz, 2014; Liu et al, 2014; Strop, 2014; Salis et al, 2015) are Streptoverticillium sp. 1.43 unit/ml, Streptoverticillium mobaraense (ajinomoto “wild type”) 1.25 unit/ml or 22 unit/mg and the yield in recombinant Escherichia coli producer may reach 19.55 unit/mg.…”

Section: Mtgs Are Expressed and Secreted Into The Human Intestinal Lumenmentioning

confidence: 99%

Transglutaminases in Dysbiosis As Potential Environmental Drivers of Autoimmunity

Lerner

Aminov

Tenbusch³

2017

Front. Microbiol.

101

View full text Add to dashboard Cite

Protein-glutamine γ-glutamyltransferases (transglutaminases, Tgs) belong to the class of transferases. They catalyze the formation of an isopeptide bond between the acyl group at the end of the side chain of protein- or peptide-bound glutamine residues and the first order 𝜀-amine groups of protein- or peptide-bound lysine. The Tgs are considered to be universal protein cross-linkers, and they play an essential role in a number of human diseases. In this review, we discuss mainly the bacterial Tgs in terms of the functionality of the enzymes and a potential role they may play in bacterial survival. Since microbial transglutaminases (mTgs) are functionally similar to the human homologs, they may be involved in the human disease provocation. We suggest here a potential involvement of Tgs in the pathologies such as autoimmune diseases. In this hypothesis, the endogenous mTgs that are secreted by the gut microbiota, especially in a dysbiotic configuration, are potential drivers of systemic autoimmunity, via the enzymatic posttranslational modification of peptides in the gut lumen. These mTg activities directed toward cross-linking of naïve proteins can potentially generate neo-epitopes that are not only immunogenic but may also activate some immune response cascades leading to the pathological autoimmune processes.

show abstract

“…4) Genetic manipulation is carried out to yield higher quantity of enzymes produced from microbial sources [28]. Some of the industrially produced enzymes produced in large scale using microorganisms as source are mentioned below in Table 1 [29][30][31]. …”

Section: Microbial Sourcesmentioning

confidence: 99%

Fermentative Production of Microbial Enzymes and their Applications: Present status and future prospects

2017

J App Biol Biotech

View full text Add to dashboard Cite

Microbial enzymes are widely used in different industries mainly because of vast availability of sources. Microbial enzymes could be genetically modified and are considered as economical in comparison to plant and animal enzymes. Production of microbial enzymes by application of fermentation procedures involves microbial propagation to get desired product. The process of fermentation is classified based on specific parameters. Microbial enzymes exhibit wide variety of applications in different industries like food, wine, dairy, baking, milling, beverages, and cereals. There are different techniques employed to produce microbial enzymes using downstream processing methods that are aimed at enzyme purification and recovery. The improvement in concentration, purity and percentage of recovery of enzymes can be achieved based on standard principles which are microbial sources, improvement of strain and application of membrane augmented downstream processing method to improve specific activity of enzyme. The article reviews on principles include microbial sources, methods of strain improvement and modern techniques associated with improvement of enzyme activity and recovery process. The application of microbial enzymes in various industries and their importance in biotechnology is highlighted.

show abstract

A novel approach for improving the yield of Bacillus subtilis transglutaminase in heterologous strains

Cited by 31 publications

References 28 publications

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Transglutaminases in Dysbiosis As Potential Environmental Drivers of Autoimmunity

Fermentative Production of Microbial Enzymes and their Applications: Present status and future prospects

Contact Info

Product

Resources

About