Heterologous expression and characterization of man gene from Bacillus Subtilis in Pichia Pastoris

Qiao, Yu; Chen, Xiaobing; Ding, Huanzhong; Yue, Ming

doi:10.1007/s11515-008-0002-5

Cited by 5 publications

(5 citation statements)

References 25 publications

(25 reference statements)

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“…The highest reported mannanase activity produced is 18,403 nkat ml -1 and was achieved by producing a B. subtilis mannanase in P. pastoris in a fermenter [4]. This compares favourably with the shake-flask-produced mannanase activity of 16,596 nkat ml -1 we report in this study.…”

Section: Discussionsupporting

confidence: 67%

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Production of the Aspergillus aculeatus endo-1,4-β-mannanase in A. niger

Zyl¹,

Moodley²,

Rose

et al. 2009

J Ind Microbiol Biotechnol

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The beta-mannanase gene (man1) from Aspergillus aculeatus MRC11624 (Izuka) was patented for application in the coffee industry. For production of the enzyme, the gene was originally cloned and expressed in Saccharomyces cerevisiae. However the level of production was found to be economically unfeasible. Here we report a 13-fold increase in enzyme production through the successful expression of beta-mannanase of Aspergillus aculeatus MRC11624 in Aspergillus niger under control of the A. niger glyceraldehyde-3-phosphate dehydrogenase promoter (gpd (P)) and the A. awamori glucoamylase terminator (glaA(T)). The effect of medium composition on mannanase production was evaluated, and it was found that the glucose concentration and the organic nitrogen source had an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16,596 nkat ml(-1) and 574 nkat mg(-1) dcw were obtained for A. niger D15[man1] when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations.

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Section: Discussionsupporting

confidence: 67%

“…3.2.1.78) belongs to the glycosyl hydrolase family #5 and has been cloned from bacterial and fungal origins [1][2][3][4]. b-mannanases catalyse the random hydrolysis of the b-1, 4-mannan main chains of mannans and heteromannans.…”

Section: Introductionmentioning

confidence: 99%

Production of the Aspergillus aculeatus endo-1,4-β-mannanase in A. niger

Zyl¹,

Moodley²,

Rose

et al. 2009

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Similar results were obtained for an antifreeze protein expressed in P. pastoris when an induction temperature of 23°C was used [34]. Until now, only Zhu et al [35] reported that lowering temperature was beneficial to β‐mannanase production in P. pastoris , but they did not discuss it in detail. In this study, we proved that a two‐stage temperature control strategy was more efficient for β‐mannanase fermentation.…”

Section: Discussionsupporting

confidence: 63%

Enhanced extracellular β‐mannanase production by overexpressing PrsA lipoprotein in Bacillus subtilis and optimizing culture conditions

Zhang

Dong

et al. 2022

J Basic Microbiol

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In this study, first, β‐mannanase gene man derived from Bacillus amyloliquefaciens CGMCC1.857 was cloned and expressed in Bacillus subtilis 168 to generate B. subtilis M1. However, the extracellular β‐mannanase activity of B. subtilis M1 was not very high. To further increase extracellular β‐mannanase extracytoplasmic molecular chaperone, PrsA lipoprotein was tandem expressed with man gene in B. subtilis 168 to yield B. subtilis M2. The secretion of β‐mannanase of B. subtilis M2 was enhanced by 15.4%, compared with the control B. subtilis M1. Subsequently, process optimization strategies were also developed to enhance β‐mannanase production by B. subtilis 168 M2. It was noted that the optimal temperature for β‐mannanase production (25°C) was different from the optimal growth temperature (37°C) for B. subtilis. Based on these findings, a two‐stage temperature control strategy was proposed where the bacterial culture was maintained at 37°C for the first 12 h to obtain a high rate of cell growth, followed by lowering the temperature to 25°C to enhance β‐mannanase production. Using this strategy, the extracellular β‐mannanase activity reached 5016 ± 167 U/ml at about 36 h, which was 19.1% greater than the best result obtained using a constant temperature (25°C). The result of this study showed that PrsA lipoprotein overexpression and two‐stage temperature control strategy were more efficient for β‐mannanase fermentation in B. subtilis.

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“…( 2001 ). Similarly, Qiao et al ( 2008 ) have used Pichia pastoris as a host for expression of MAN gene of Bacillus subtilis . It has been observed that, if the same gene encoding mannanase is expressed in different hosts, the resultant recombinant enzymes show somewhat different properties.…”

Section: Heterologous Productionmentioning

confidence: 99%

Microbial Mannanases: Properties and Applications

Soni

Kango

2013

Advances in Enzyme Biotechnology

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Mannans are a major constituent of the hemicellulose fraction of lignocelluloses. Mannans perform distinct functions as structural components in cell walls of softwoods and storage functions in seeds. Enzymatic hydrolysis of mannan involves the backbone hydrolyzing endo-β-mannanases and β-mannosidases. Mannans are heteropolymeric and their hydrolysis also requires the action of β-glucosidases and side-chain cleaving α-galactosidases and acetyl mannan esterases. Microorganisms are therefore explored for the production of such repertoire of enzymes so that effective mannan hydrolysis can be achieved. The present chapter discusses the occurrence and structural properties of mannans in plant materials and its hydrolysis using enzymes sourced from various fungi and other microorganisms. The production and properties of mannanolytic enzymes, their cloning and expression in heterologous hosts, and their application have also been discussed .

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Heterologous expression and characterization of man gene from Bacillus Subtilis in Pichia Pastoris

Cited by 5 publications

References 25 publications

Production of the Aspergillus aculeatus endo-1,4-β-mannanase in A. niger

Production of the Aspergillus aculeatus endo-1,4-β-mannanase in A. niger

Enhanced extracellular β‐mannanase production by overexpressing PrsA lipoprotein in Bacillus subtilis and optimizing culture conditions

Microbial Mannanases: Properties and Applications

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