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Secretion of Streptomyces mobaraensis pro-transglutaminase by coryneform bacteria.

Itaya H, Kikuchi Y - Appl. Microbiol. Biotechnol. (2008)

Bottom Line: We previously reported on the secretion of Streptomyces mobaraensis transglutaminase by Corynebacterium glutamicum ATCC13869 (formerly classified as Brevibacterium lactofermentum).We found that most coryneform species secreted pro-transglutaminase efficiently.Moreover, we confirmed that Corynebacterium ammoniagenes ATCC6872 produced about 2.5 g/l pro-transglutaminase over a 71-h period in a jar fermentor.

View Article: PubMed Central - PubMed

Affiliation: Institute of Life Sciences, Ajinomoto Co. Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki 210-8681, Japan.

ABSTRACT
We previously reported on the secretion of Streptomyces mobaraensis transglutaminase by Corynebacterium glutamicum ATCC13869 (formerly classified as Brevibacterium lactofermentum). In the present work, we investigated whether any other coryneform bacteria showed higher productivity than C. glutamicum ATCC13869. We found that most coryneform species secreted pro-transglutaminase efficiently. Moreover, we confirmed that Corynebacterium ammoniagenes ATCC6872 produced about 2.5 g/l pro-transglutaminase over a 71-h period in a jar fermentor. Our findings suggest that some other coryneform bacteria, especially C. ammoniagenes ATCC6872, are potential hosts for industrial scale protein production.

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Effect of signal peptide sequence on pro-TG secretion in coryneform bacteria. a Amino acid sequence alignment of C. ammoniagenes CspA signal peptide and C. glutamicum CspB signal peptide using Vector NTI software. Identical and similar residues are shown on black and gray backgrounds, respectively. b Accumulation of secreted pro-TG by coryneform bacteria carrying pPSPTG1 or pPKPTG1. The solid bars indicate pro-TG accumulation using the CspA signal peptide from C. ammoniagenes ATCC6872, and the open bars indicate pro-TG accumulation using the CspB signal peptide from C. glutamicum ATCC13869
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Fig2: Effect of signal peptide sequence on pro-TG secretion in coryneform bacteria. a Amino acid sequence alignment of C. ammoniagenes CspA signal peptide and C. glutamicum CspB signal peptide using Vector NTI software. Identical and similar residues are shown on black and gray backgrounds, respectively. b Accumulation of secreted pro-TG by coryneform bacteria carrying pPSPTG1 or pPKPTG1. The solid bars indicate pro-TG accumulation using the CspA signal peptide from C. ammoniagenes ATCC6872, and the open bars indicate pro-TG accumulation using the CspB signal peptide from C. glutamicum ATCC13869

Mentions: Next, to investigate whether the secretion efficiency depended on the signal peptide sequence, we examined the effect of using the CspA signal peptide from C. ammoniagenes ATCC6872 (Fig. 2a) or the CspB signal peptide from C. glutamicum ATCC13869 (Fig. 2a) for the pro-TG secretion. C. ammoniagenes ATCC6872, C. acetoacidophilum ATCC13870, C. glutamicum ATCC14020, M. ammoniaphilum ATCC15354, and C. callunae ATCC15991 could efficiently secrete the pro-TG using the CspA signal peptide from C. ammoniagenes ATCC6872 in this study. These strains and C. glutamicum ATCC13869 were transformed with pPKPTG1 harboring the CspB signal peptide from C. glutamicum ATCC13869. As shown in Fig. 2b, the substitution of the CspB signal peptide had little effect on pro-TG accumulation in C. acetoacidophilum ATCC13870, C. glutamicum ATCC14020, and M. ammoniaphilum ATCC15354. However, in C. callunae ATCC15991, the pro-TG accumulation (403 mg/l) was approximately halved (746 mg/l) while in C. ammoniagenes ATCC6872, it was about 2.8-fold higher.Fig. 2


Secretion of Streptomyces mobaraensis pro-transglutaminase by coryneform bacteria.

Itaya H, Kikuchi Y - Appl. Microbiol. Biotechnol. (2008)

Effect of signal peptide sequence on pro-TG secretion in coryneform bacteria. a Amino acid sequence alignment of C. ammoniagenes CspA signal peptide and C. glutamicum CspB signal peptide using Vector NTI software. Identical and similar residues are shown on black and gray backgrounds, respectively. b Accumulation of secreted pro-TG by coryneform bacteria carrying pPSPTG1 or pPKPTG1. The solid bars indicate pro-TG accumulation using the CspA signal peptide from C. ammoniagenes ATCC6872, and the open bars indicate pro-TG accumulation using the CspB signal peptide from C. glutamicum ATCC13869
© Copyright Policy
Related In: Results  -  Collection

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Fig2: Effect of signal peptide sequence on pro-TG secretion in coryneform bacteria. a Amino acid sequence alignment of C. ammoniagenes CspA signal peptide and C. glutamicum CspB signal peptide using Vector NTI software. Identical and similar residues are shown on black and gray backgrounds, respectively. b Accumulation of secreted pro-TG by coryneform bacteria carrying pPSPTG1 or pPKPTG1. The solid bars indicate pro-TG accumulation using the CspA signal peptide from C. ammoniagenes ATCC6872, and the open bars indicate pro-TG accumulation using the CspB signal peptide from C. glutamicum ATCC13869
Mentions: Next, to investigate whether the secretion efficiency depended on the signal peptide sequence, we examined the effect of using the CspA signal peptide from C. ammoniagenes ATCC6872 (Fig. 2a) or the CspB signal peptide from C. glutamicum ATCC13869 (Fig. 2a) for the pro-TG secretion. C. ammoniagenes ATCC6872, C. acetoacidophilum ATCC13870, C. glutamicum ATCC14020, M. ammoniaphilum ATCC15354, and C. callunae ATCC15991 could efficiently secrete the pro-TG using the CspA signal peptide from C. ammoniagenes ATCC6872 in this study. These strains and C. glutamicum ATCC13869 were transformed with pPKPTG1 harboring the CspB signal peptide from C. glutamicum ATCC13869. As shown in Fig. 2b, the substitution of the CspB signal peptide had little effect on pro-TG accumulation in C. acetoacidophilum ATCC13870, C. glutamicum ATCC14020, and M. ammoniaphilum ATCC15354. However, in C. callunae ATCC15991, the pro-TG accumulation (403 mg/l) was approximately halved (746 mg/l) while in C. ammoniagenes ATCC6872, it was about 2.8-fold higher.Fig. 2

Bottom Line: We previously reported on the secretion of Streptomyces mobaraensis transglutaminase by Corynebacterium glutamicum ATCC13869 (formerly classified as Brevibacterium lactofermentum).We found that most coryneform species secreted pro-transglutaminase efficiently.Moreover, we confirmed that Corynebacterium ammoniagenes ATCC6872 produced about 2.5 g/l pro-transglutaminase over a 71-h period in a jar fermentor.

View Article: PubMed Central - PubMed

Affiliation: Institute of Life Sciences, Ajinomoto Co. Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki 210-8681, Japan.

ABSTRACT
We previously reported on the secretion of Streptomyces mobaraensis transglutaminase by Corynebacterium glutamicum ATCC13869 (formerly classified as Brevibacterium lactofermentum). In the present work, we investigated whether any other coryneform bacteria showed higher productivity than C. glutamicum ATCC13869. We found that most coryneform species secreted pro-transglutaminase efficiently. Moreover, we confirmed that Corynebacterium ammoniagenes ATCC6872 produced about 2.5 g/l pro-transglutaminase over a 71-h period in a jar fermentor. Our findings suggest that some other coryneform bacteria, especially C. ammoniagenes ATCC6872, are potential hosts for industrial scale protein production.

Show MeSH