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Kerovuo, Janne; Weymarn, Niklas von; Povelainen, Mira; Auer, Sanna; Miasnikov, Andrei N.

doi:10.1023/a:1005694731039

Cited by 23 publications

(7 citation statements)

References 15 publications

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“…Sodium phytate was included as a Replacing calcium on both the enzyme and phytate with other cations revealed about 20-23% activity with Mg 2+ and Sr 2+ at 37°C but not at 70°C. Oh et al [28] have earlier shown partial activation of Bacillus DS11 phytase with Sr 2+ but not with any other cation [8]. These results indicate the importance of Ca 2+ on the substrate for providing optimal activity.…”

Section: °C 70°cmentioning

confidence: 79%

“…The enzyme was expressed at high level in E. coli and purified using a simple procedure exploiting its thermostability and affinity to metal ions via the histidine tag. Characterization of the enzyme showed that its physico-chemical properties such as molecular weight, specific activity, optimal pH and temperature of activity are in the range known for Bacillus phytases [4,6,7,15,27,28]. Although Bacillus phytases have low specific activity compared to the commercially available acidic phytases, they are more thermostable and can withstand the high temperature of feed pelleting, they are active on the metal-phytate complexes in small intestine of the monogastric animals, and they are resistant to calcium and phosphate inhibition [4,[11][12][13].…”

Section: °C 70°cmentioning

confidence: 99%

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Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

Tran

Hashim

Gaber

et al. 2011

Journal of Inorganic Biochemistry

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Section: °C 70°cmentioning

confidence: 79%

Section: °C 70°cmentioning

confidence: 99%

Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

Tran

Hashim

Gaber

et al. 2011

Journal of Inorganic Biochemistry

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“…For B. subtilis a similar phosphate controlled expression system based on the pst promoter was suggested [10]. However, a crucial starvation of an essential substrate, such as phosphate, during the protein over-production phase could diminish the protein synthesis capacity of the host.…”

Section: Discussionmentioning

confidence: 99%

“…Data of this study indicated that the expression system using the phyL promoter is not only strong and tightly regulated by the level of inorganic phosphate but also easily inducible by the alternative phosphate source phytate. The suggested promoter system is comparable to the pst promoter system of B. subtilis [10] but exhibits an additional feature due to its expression stimulation by the alternative phosphate source phytate.…”

Section: Discussionmentioning

confidence: 99%

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An auto-inducible phosphate-controlled expression system of Bacillus licheniformis

et al. 2019

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BackgroundA promoter that drives high-level, long-term expression of the target gene under substrate limited growth conditions in the absence of an artificial inducer would facilitate the efficient production of heterologous proteins at low cost. A novel phosphate-regulated expression system was constructed using the promoter of the phytase encoding gene phyL from Bacillus licheniformis for the overexpression of proteins in this industrially relevant host.ResultsIt is shown that the phyL promoter enables a strong overexpression of the heterologous genes amyE and xynA in B. licheniformis when cells were subjected to phosphate limitation. Whether B. licheniformis can use phytate as an alternative phosphate source and how this substrate influences the PphyL controlled gene expression under growth conditions with limited inorganic phosphate concentrations were also investigated. It is shown that B. licheniformis cells are able to use sodium phytate as alternative phosphate source. The addition of small amounts of sodium phytate (≤ 5 mM) to the growth medium resulted in a strong induction and overexpression of both model genes in B. licheniformis cells under phosphate limited growth conditions.ConclusionsThe PphyL controlled expression of the investigated heterologous genes in B. licheniformis is strongly auto-induced under phosphate limited conditions. The proposed PphyL expression system enables an overexpression of target genes in B. licheniformis under growth conditions, which can be easily performed in a fed-batch fermentation process.Electronic supplementary materialThe online version of this article (10.1186/s12896-018-0490-6) contains supplementary material, which is available to authorized users.

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Production of D‐arabitol by a metabolic engineered strain of Bacillus subtilis

Povelainen¹,

Miasnikov²

2006

Biotechnology Journal

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A novel method for D-arabitol production with a metabolically engineered Bacillus subtilis strain is described. A known transketolase-deficient and D-ribose-producing mutant of B. subtilis (ATCC 31094) was further modified by disruption of its rpi (D-ribose phosphate isomerase) gene to create a D-ribulose- and D-xylulose-producing B. subtilis strain. Expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain resulted in a strain of B. subtilis capable of converting D-glucose to D-arabitol with a high yield (38%) and little by-product formation.

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Untitled

Cited by 23 publications

References 15 publications

Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

An auto-inducible phosphate-controlled expression system of Bacillus licheniformis

Production of D‐arabitol by a metabolic engineered strain of Bacillus subtilis

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