Cloning and expression of the transglutaminase gene from Streptoverticillium ladakanum in Streptomyces lividans

Lin, Yi-Sin; Chao, Mei-Li; Liu, Chang-Hsiesh; Chu, Wen-Shen

doi:10.1016/s0032-9592(03)00134-1

Cited by 32 publications

(26 citation statements)

References 34 publications

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“…The purified recombinant MtgA was not affected by Ca +2 or EDTA, suggesting that it is calciumindependent, similar to those purified from Streptoverticillium species [26,29] and B. subtilis [28]. The enzymatic reaction catalyzed by TGases of vertebrates and some invertebrates require Ca +2 to expose a cysteine residue in the active site [10].…”

Section: Effects Of Metal Cations and Inhibitorsmentioning

confidence: 64%

“…MTGase activity was determined by a colorimetric hydroxamate procedure using N-carbobenzoxy-L-glutaminyl-glycine as a substrate [29]. A calibration curve was prepared with L-glutamic acid-c-monohydroxamic acid.…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…ladakanum B1 [29], and B. subtilis [28] have been cloned and sequenced. Several expression systems including S. lividans [29,30], Escherichia coli [31], and Corynebacterium glutamicum [32] have been used for the production of recombinant MTGases. However, with the exception of the C. glutamicum system, the expression levels of recombinant MTGases are very low [32].…”

Section: Introductionmentioning

confidence: 99%

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Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Lin

Hsieh

Lai

et al. 2008

J Ind Microbiol Biotechnol

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Recombinant Streptomyces platensis transglutaminase (MtgA) produced by the Streptomyces lividans transformant 25-2 was purified by ammonium sulfate fractionation, followed by CM-Sepharose CL-6B fast flow, and blue-Sepharose fast flow chromatography. The purification factor was approximately 33.2-fold, and the yield was 65%. The molecular weight of the purified recombinant MtgA was 40.0 KDa as estimated by SDS-PAGE. The optimal pH and the temperature for the enzyme activity were 6.0 and 55 degrees C, respectively, and the enzyme was stable at pH 5.0-6.0 and at temperature 45-55 degrees C. Enzyme activity was not affected by Ca(2+), Li(+), Mn(2+), Na(+), Fe(3+), K(+), Mg(2+), Al(3+), Ba(2+), Co(2+), EDTA, or IAA but was inhibited by Fe(2+), Pb(2+), Zn(2+), Cu(2+), Hg(2+), PCMB, NEM, and PMSF. Optimization of the fermentation medium resulted in a twofold increase of recombinant MtgA activity in both flasks (5.78 U/ml) and 5-l fermenters (5.39 U/ml). Large-scale productions of the recombinant MtgA in a 30-l air-lift fermenter and a 250-l stirred-tank fermenter were fulfilled with maximal activities of 5.36 and 2.54 U/ml, respectively.

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Section: Effects Of Metal Cations and Inhibitorsmentioning

confidence: 64%

Section: Enzyme Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Lin

Hsieh

Lai

et al. 2008

J Ind Microbiol Biotechnol

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“…However, S. ladakanum and S. lividans could not produce MTGase for none of the culture mediums, temperatures and pH value. Some researchers attempted to produce MTGase by genetic modification methods from S. ladakanum and S. lividans strains which produce MTGase very slightly [18,19]. On the other hand, according to the Tellez-Luis et al [20], S. ladakanum is able to produce MTGase (0.725 U/ml) in the presence of casein and glycerol in the broth medium.…”

Section: Resultsmentioning

confidence: 99%

Enhancement of microbial transglutaminase production from

Turker¹,

Domurcuk²,

Tokatlı³

et al. 2016

Ukr. food j.

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“…This approach involves cloning and over expression of genes encoding bacterial proteins. Lin et al (2004Lin et al ( , 2006 reported the success of cloning and expression of MTGaseencoding genes derived from S. platensis and S.ladakanum in S. lividans host. The MTGase gene expression is regulated by a native promoter that controls MTGase gene from S. lividans.…”

Section: Introductonmentioning

confidence: 99%

Cloning of a Transglutaminase Gene from an Indonesian Streptomyces Strain

Seprianto

Zilda²,

Fawzya³

et al. 2016

Squalen Bull. Marine Fisheries Postharvest Biotech.

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Microbial Transglutaminase (MTGase, EC 2.3.2.13) is an enzyme that catalyzes the transfer of acyl group. It has tremendous applications in binding meats together in texture improvement process. This research was aimed at cloning MTGase gene from Streptomyces thioluteus TTA 02 SDS 14. A genomic library with the average of 40 kb insert size was initially generated from the total genomic DNA of S.thioluteus TTA 02 SDS 14, and was subsequently screened using an MTGase-targeting primer pair. The genomic library construction was based on the fosmid pCC1FOS TM hosted in E.coli EPI300-TI R . The isolated positive clone was verified by enzymatic digestion with NotI, EcoRV, and BamHI, followed by PCR-amplification of MTGase fragment. The PCR product result of 360 bp was sequenced. The sequence analysis strongly suggests that the positive clone with 40-kb insert harbors an MTGase gene.

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Cloning and expression of the transglutaminase gene from Streptoverticillium ladakanum in Streptomyces lividans

Cited by 32 publications

References 34 publications

Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Enhancement of microbial transglutaminase production from

Cloning of a Transglutaminase Gene from an Indonesian Streptomyces Strain

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