Synthesis of poly (γ-glutamic acid) and heterologous expression of pgsBCA genes

Cao, Mingfeng; Song, Chunyan; Jin, Yinghong; Liu, Li; Liu, Jing; Xie, Hengkun; Guo, Wenbin; Wang, Shufang

doi:10.1016/j.molcatb.2010.07.014

Cited by 40 publications

(32 citation statements)

References 26 publications

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“…The L-glutamic-aciddependent bacteria include B. subtilis (chungkookjang) (Ashiuchi et al, 2001a), B. licheniformis 9945a (Birrer et al, 1994) B. subtilis CGMCC 0833 , B. licheniformis NK-03 (Cao et al, 2010) and B. subtilis (natto) ATCC 15245 (Bhat et al, 2013), whilst the non-Lglutamic-acid-dependent producers include B. subtilis C1 (Shih et al, 2005), B. amyloliquefaciens LL3 (Cao et al, 2011) and B. subtilis C10 (Zhang et al, 2012). For Lglutamic-acid-dependent bacteria, the PGA yield increases with an increase in the L-glutamic acid concentration in the medium.…”

Section: Production Of C-pga By Microbial Fermentationmentioning

confidence: 99%

Poly-γ-glutamic acid: production, properties and applications

et al. 2015

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Section: Production Of C-pga By Microbial Fermentationmentioning

confidence: 99%

Poly-γ-glutamic acid: production, properties and applications

et al. 2015

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“…It was previously reported that tobacco leaf cells (Tarui et al ., 2005) and the glutamate-producing Corynebacterium glutamicum strains harbouring pgsBCA expression vectors could display γ-PGA synthetase and accumulate extracellular γ-PGA without L-glutamate (Sung et al ., 2003; Cao et al ., 2010). Cao et al .…”

Section: Introductionmentioning

confidence: 99%

Engineering of recombinant Escherichia coli cells co‐expressing poly‐γ‐glutamic acid (γ‐PGA) synthetase and glutamate racemase for differential yielding of γ‐PGA

Cao

Geng

Zhang

et al. 2013

Microbial Biotechnology

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Poly-γ-glutamic acid (γ-PGA) is a promising environmental-friendly material with outstanding water solubility, biocompatibility and degradability. However, it is tough to determine the relationship between functional synthetic enzyme and the strains' yield or substrate dependency. We cloned γ-PGA synthetase genes pgsBCA and glutamate racemase gene racE from both L-glutamate-dependent γ-PGA-producing Bacillus licheniformis NK-03 and L-glutamate-independent B. amyloliquefaciens LL3 strains. The deduced RacE and PgsA from the two strains shared the identity of 84.5% and 78.53%, while PgsB and PgsC possessed greater similarity with 93.13% and 93.96%. The induced co-expression of pgsBCA and racE showed that the engineered Escherichia coli strains had the capacity of synthesizing γ-PGA, and LL3 derived PgsBCA had higher catalytic activity and enhanced productivity than NK-03 in Luria–Bertani medium containing glucose or L-glutamate. However, the differential effect was weakened when providing sufficient immediateness L-glutamate substrate, that is, the supply of substrate could be served as the ascendance upon γ-PGA production. Furthermore, RacE integration could enhance γ-PGA yield through improving the preferred d-glutamate content. This is the first report about co-expression of pgsBCA and racE from the two Bacillus strains, which will be of great value for the determination of the biosynthetic mechanism of γ-PGA.

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“…With outstanding water solubility, biocompatibility, and degradability, ␥-PGA is widely used in medicine, cosmetics, food, and wastewater treatment (14). The known ␥-PGA producers with high productivity are mostly L-glutamic acid dependent; however, the strains not requiring glutamic acid are of great interest in the search for lower costs and a simplified process in industrial systems (5).…”

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confidence: 99%