Efficient soluble expression of secreted matrix metalloproteinase 26 in Brevibacillus choshinensis

Mu, Tianyang; Liang, Weiguo; Ju, Ying; Wang, Zhiyong; Wang, Zhongyuan; Roycik, Mark D.; Sang, Qing‐Xiang Amy; Yu, Dahai; Xiang, Hongyu; Fang, Xuexun

doi:10.1016/j.pep.2013.07.012

Cited by 11 publications

(10 citation statements)

References 42 publications

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“…To the best of our knowledge, there are few medium used for Brevibacillus choshinensis fermentation, which mainly includes 2SY [22,23], TM [22,23,31,32], and TM-derived medium [36]. When expressed using 2SY medium, the pullulanase activity was 24.3 U/mL, which was only 49.2 % of that obtained with TM medium.…”

Section: Optimization Of the Culture Medium Employing Single-factor Rmentioning

confidence: 96%

“…The Brevibacillus choshinensis (formerly Bacillus brevis) expression system has been developed for highly efficient production of heterologous proteins, including cellulase [18], metalloproteinase [23], and VHH antibody [22]. Brevibacillus choshinensis, a gram-positive bacterium, has exceptional capacity for extracellular protein secretion that is particularly suitable for the production of secretory proteins [15,21,25].…”

Section: Introductionmentioning

confidence: 99%

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Efficient extracellular expression of Bacillus deramificans pullulanase in Brevibacillus choshinensis

Zou

Duan

2016

Journal of Industrial Microbiology and Biotechnology

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In this study, the pullulanase gene from Bacillus deramificans was efficiently expressed in Brevibacillus choshinensis. The optimal medium for protein expression was determined through a combination of single-factor experiments and response surface methodology. The initial pH of the medium and the culture temperature were optimized. The pullulanase yield increased 10.8-fold through medium and condition optimization at the shake-flask level. From the results of these experiments, the dissolved oxygen level was optimized in a 3-L fermentor. Under these optimized conditions, the pullulanase activity and the specific pullulanase productivity reached 1005.8 U/mL and 110.5 × 10(3) U/g dry cell weight, respectively, with negligible intracellular expression. The Brevibacillus choshinensis expression system has proven to be valuable for the extracellular production of pullulanase.

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Section: Optimization Of the Culture Medium Employing Single-factor Rmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Efficient extracellular expression of Bacillus deramificans pullulanase in Brevibacillus choshinensis

Zou

Duan

2016

Journal of Industrial Microbiology and Biotechnology

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“…Pet25b-His (6× histidine-tagged expression vector) was selected as the vector, and BamHI, XhoI as the restriction sites. The successfully constructed plasmids were transferred to Escherichia coli competent cells (E.coli rosetta, DE3) (Novagen, Beijing, China) [50]. E.coli rosetta (DE3) as an expression host was transformed and cultured in the LB medium (100 µg/mL chloramphenicol or 100 µg/mL ampicillin) at 37 • C overnight with shaking.…”

Section: Induction and Expression Of Proteinsmentioning

confidence: 99%

A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2

Meng

Wang

Lan

et al. 2019

IJMS

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Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_1434 containing the 6× His-tag produced in Escherichia coli (hereinafter termed Amuc_1434*) was isolated to homogeneity and biochemically characterised. Results showed that the enzyme can hydrolyse hemoglobin with an activity of 17.21 U/μg. The optimal pH and temperature for hemoglobin hydrolysis of Amuc_1434* were found to be around 8.0 and 40 °C, respectively. Amuc_1434* is identified as a member of the aspartic protease family through the action of inhibitor pepstatin A. Amuc_1434* promotes the adhesion of colon cancer cell line LS174T, which can highly express Muc2. Significantly Amuc_1434* can degrade Muc2 of colon cancer cells. Amuc_1434 is mainly located in the colon of BALB/c mice. These results suggest that the presence of Amuc_1434 from Akkermansia muciniphila may be correlated with the restoration of gut barrier function by decreasing mucus layer thickness.

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“…[3][4][5][6] In recent years, research on MMP-26 has focused on its role as a tumor marker, identifying its substrates and regulation of MMP-26 gene expression. 7,8 These studies have provided considerable information on MMP-26; however, the biological function of MMP-26 remains unclear. Several studies have shown that MMP-26 is largely expressed within the cell and seldom secreted extracellularly.…”

Section: Introductionmentioning

confidence: 99%

Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26

Zhang

et al. 2019

RSC Adv.

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Efficient soluble expression of secreted matrix metalloproteinase 26 in Brevibacillus choshinensis

Cited by 11 publications

References 42 publications

Efficient extracellular expression of Bacillus deramificans pullulanase in Brevibacillus choshinensis

Efficient extracellular expression of Bacillus deramificans pullulanase in Brevibacillus choshinensis

A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2

Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26

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