Expression of recombinant endochitinase from the Antarctic bacterium, Sanguibacter antarcticus KOPRI 21702 in Pichia pastoris by codon optimization

Lee, Sung Gu; Koh, Hye Yeon; Han, Se Jong; Park, Heeyong; Na, Deuk Chae; Kim, Il-Chan; Lee, Hong Kum; Yim, Joung Han

doi:10.1016/j.pep.2010.01.017

Cited by 30 publications

(17 citation statements)

References 29 publications

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“…(30 °C) (Bendt et al, 2001), S. antarcticus (37 °C) (Lee et al, 2010), and S. maltophilia (40 °C) (Suma & Podile, 2013). However, the optimal temperature of PbChi70 is lower than those of several chitinases from B. cereus IO8 (65 °C, Hammami et al, 2013), B. licheniformis (65 °C) (Sandalli et al, 2008), and T. chitonophagus (80 °C) (Andronopoulou & Vorgias, 2004).…”

Section: Effect Of Ph and Temperature On The Activity And Stability Omentioning

confidence: 99%

“…In addition, there are several chitinases which are optimally active at alkaline pH 7.5-9.0 (Bendt et al, 2001;Lee et al, 2010). Generally, chitinases have optimal temperatures at a range of 20-50 °C and are stable up to 55 °C (Bhattacharya et al, 2007).…”

Section: Effect Of Ph and Temperature On The Activity And Stability Omentioning

confidence: 99%

“…GC72 (Gao, Zhang, Chen, Hao, Tong, & Ouyang, 2015), Laceyella putida (Shibasaki, Uchimura, Miura, Kobayashi, Usami, & Horikoshi, 2014) and Massilia timonae (Adrangi, Faramarzi, Shahverdi, & Sepehrizadeh, 2010). Moreover, many chitinase genes from Bacillus halodurans (da Silva, García-Fraga, López-Seijas, & Sieiro, 2014), B. licheniformis (Sandalli, Kacagan, Canakci, & Belduz, 2008;Songsiriritthigul, Lapboonrueng, Pechsrichuang, Pesatcha, & Yamabhai, 2010), Chitiniphilus shinanonensis (Huang, Shizume, Nogawa, Taguchi, & Shimosaka, 2012), Paenibacillus barengoltzii (Fu, Yan, Yang, Yang, Guo, & Jiang, 2014), Pseudoalteromonas tunicate (García-Fraga et al, 2015), Sanguibacter antarcticus (Lee et al, 2010), Serratia proteamaculans (Purushotham & Podile, 2012), and Vibrio sp. (Bendt et al, 2011) have been cloned and heterologously expressed.…”

Section: Introductionmentioning

confidence: 99%

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Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii

et al. 2016

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Section: Effect Of Ph and Temperature On The Activity And Stability Omentioning

confidence: 99%

Section: Effect Of Ph and Temperature On The Activity And Stability Omentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii

et al. 2016

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“…FfIBP의 이종발현은 플라즈미드 벡터 pPICZαA (Invitrogen, Carlsbad, CA, USA)와 호스트 균주 Pichia pastoris X-33 (Invitrogen, Carlsbad, CA, USA)에서 수행하였다 [12]. (Fig.…”

Section: 균주 및 배지unclassified

Production of Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by using Fed-batch Culture of Recombinant Pichia pastoris

김은재¹,

도학원²,

이준혁³

et al. 2014

KSBB Journal

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Antifreeze proteins (AFP) inhibit ice growth to permit the survival of polar organisms in the cold environments. The recombinant AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris icebinding protein), was produced using Pichia pastoris expression system. The optimum fermentation temperature (30 o C) and pH (5) for FfIBP production were determined using a fedbatch culture system. The maximal cell density and purified FfIBP were 112 g/L and 70 mg/L, respectively. The thermal hysteresis (TH) activity (0.85) of FfIBP obtained using a glycerol-methanol fed-batch culture system was 2-fold higher than that of the LeIBP (Leucosporidium ice-binding protein). This work allows for large-scale production of FfIBP, which could be extended to further application studies using recombinant AFPs.

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“…Codon optimization, indeed, is to alter rare codons in target gene so as to adapt them to the codon usage of specific expression host. Recently, a huge number of studies have reported an increase in expression levels by codon optimization (Gustafsson, Govindarajan et al 2004;Zhou, Schnake et al 2004;Lee, Koh et al 2010). Here, we explored codon optimization of Col H gene to express in E. coli.…”

Section: Introductionmentioning

confidence: 99%

Codon optimization of Col H gene encoding Clostridium histolyticum collagenase to express in Escherichia coli

Alipour

Raz

Djadid

et al. 2014

Preprint

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A given amino acid sequence can be encoded by a huge number of different nucleic acid sequences. These sequences, however, prove not to be equally useful. The choice of sequence can significantly impact the expression of an encoded protein. As regards the importance of protein-coding sequence and promising industrial and medicinal applications of Clostridium histolyticum collagenase, this study examined the codon optimization of the Col H gene so as to enhance collagenase expression in Escherichia coli (E. coli). The coding region of mature Col H gene was optimized according to the codon usage of E. coli using Gene Designer software (DNA 2.0). The results revealed that relative frequency of codon usage in Col H gene was adapted to the most preferred triplets in E. coli in such a way that codon usage bias in E. coli was enhanced after codon optimization. Similarly, the higher level of collagenase expression was more likely the result of substituting rare codons with optimal codons. As has been reported elsewhere, the findings from this study suggest that codon optimization provides a theoretical improvement in Col H gene expression in E. coli.In spite of that, experimental research is needed to confirm the improvement.PeerJ PrePrints | http://dx.doi.org/10.7287/peerj.preprints.754v1 | CC-BY 4.0 Open Access |

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Expression of recombinant endochitinase from the Antarctic bacterium, Sanguibacter antarcticus KOPRI 21702 in Pichia pastoris by codon optimization

Cited by 30 publications

References 29 publications

Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii

Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii

Production of Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by using Fed-batch Culture of Recombinant Pichia pastoris

Codon optimization of Col H gene encoding Clostridium histolyticum collagenase to express in Escherichia coli

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