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Kaushal, Anju; Pabbi, Sunil; Sharma, Prince

doi:10.1023/a:1025133401307

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Heterologous Expression Of α-Acetolactate Synthase and α-Acetolactate Decarboxylase And Production Of Acetoin In B Methanolicus1

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Cited by 6 publications

(1 citation statement)

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“…57 Contrarily, for the acetolactate synthase BudB in E. cloacae and AlsS in B. licheniformis the optimal temperature has been found to be 37 °C. 58,59 No comparable data is available for the second enzyme of the pathway, acetolactate decarboxylase (AlsD), but our results indicate that AlsD from B. subtilis retains activity at 50 °C. MGA3 acet Bs , MGA3 acet Bl and MGA3 acet Ec were then tested for the production of acetoin.…”

Section: Heterologous Expression Of α-Acetolactate Synthase and α-Acetolactate Decarboxylase And Production Of Acetoin In B Methanolicusmentioning

confidence: 77%

Methanol-based acetoin production by genetically engineeredBacillus methanolicus

et al. 2020

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Section: Heterologous Expression Of α-Acetolactate Synthase and α-Acetolactate Decarboxylase And Production Of Acetoin In B Methanolicusmentioning

confidence: 77%

Methanol-based acetoin production by genetically engineeredBacillus methanolicus

et al. 2020

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Acetolactate synthase (AlsS) in Bacillus licheniformis WX-02: enzymatic properties and efficient functions for acetoin/butanediol and l-valine biosynthesis

Huo

Zhan

Wang

et al. 2017

Bioprocess Biosyst Eng

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Acetolactate synthase catalyzes two molecules of pyruvates to form α-acetolactate, which is further converted to acetoin and 2,3-butanediol. In this study, by heterologous expression in Escherichia coli, the enzymatic properties of acetolactate synthase (AlsS) from Bacillus licheniformis WX-02 were characterized. Its K and k for pyruvate were 3.96 mM and 514/s, respectively. It has the optimal activity at pH 6.5, 37 °C and was feedback inhibited by L-valine, L-leucine and L-isoleucine. Furthermore, the alsS-deficient strain could not produce acetoin, 2,3-butanediol, and L-valine, while the complementary strain was able to restore these capacities. The alsS overexpressing strain produced higher amounts of acetoin/2,3-butanediol (57.06 g/L) and L-valine (2.68 mM), which were 10.90 and 92.80% higher than those of the control strain, respectively. This is the first report regarding the in-depth understanding of AlsS enzymatic properties and its functions in B. licheniformis, and overexpression of AlsS can effectively improve acetoin/2,3-butanediol and L-valine production in B. licheniformis. We envision that this AlsS can also be applied in the improvement of acetoin/2,3-butanediol and L-valine production in other microbes.

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Improvement on bioprocess economics for 2,3-butanediol production from very high polarity cane sugar via optimisation of bioreactor operation

Maina

Stylianou

Vogiatzi

et al. 2019

Bioresource Technology

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Untitled

Cited by 6 publications

References 28 publications

Methanol-based acetoin production by genetically engineeredBacillus methanolicus

Methanol-based acetoin production by genetically engineeredBacillus methanolicus

Acetolactate synthase (AlsS) in Bacillus licheniformis WX-02: enzymatic properties and efficient functions for acetoin/butanediol and l-valine biosynthesis

Improvement on bioprocess economics for 2,3-butanediol production from very high polarity cane sugar via optimisation of bioreactor operation

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