Production of Nitrilase by a Recombinant Escherichia coli in a Laboratory Scale Bioreactor

Jain, Deepak Kumar; Meena, Vachan Singh

doi:10.4172/2167-7972.1000103

Cited by 4 publications

(1 citation statement)

References 22 publications

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“…While, the pH at 200 rpm reduced slightly to 6.41 ± 0.26 at 120 h of fermentation. According to a study conducted by Jain et al [47], they remarked that an increased in agitation speed caused the sheardependent mechanism that was directly affected the growth and xylanase production. …”

Section: Optimisation Of Agitation Speed On Xylanase Production By Asmentioning

confidence: 99%

Bioprocessing of Agricultural Wastes as Optimised Carbon Source and Optimisation of Growth Conditions for Xylanase Production by Aspergillus brasiliensis in Agitated Solid State Fermentation (Ssf)

Lau²

2014

J Biodivers Biopros Dev

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Objective: Xylanase has been involved in many industrial applications especially in the pulp and paper, baking, detergent as well as food and beverage industries. This enzyme is produced by various microorganisms, mainly from fungal species. Therefore, in this study, Aspergillus brasiliensis ATCC 16404 was investigated for the optimum xylanase production under agitated solid state fermentation (SsF) using different agricultural wastes as alternative inexpensive carbon source. Methods:A. brasiliensis was cultured in 10 g agricultural waste with addition of 2% yeast extract as the nitrogen source up to 120 h of SsF to elucidate xylanase production. Effect of various agricultural wastes such as wheat bran, rice bran, soybean hulls, barley husk, maize and palm kernel cake (PKC) on xylanase activity were enumerated in a stepwise manner, where one parameter was investigated at a time approach to obtain the optimum carbon source for the maximum xylanase production by A. brasiliensis. Thereafter, growth temperatures from 25 to 45°C, initial medium pH from 4 to 10 and agitation speeds of 50 to 200 rpm were also elucidated to determine the optimum growth conditions for the maximum production of xylanase by A. brasiliensis.Results: Based on our results, the highest xylanase activity of 7.30 ± 1.93 U/mL was obtained using wheat bran as the prime carbon source with the initial medium pH 6.5 at 30°C at the agitation speed of 150 rpm. Conclusion:Thus, in our study, the maximum xylanase production by A. brasiliensis using solid state bioprocessing of wheat bran as the carbon source was achieved with the addition of 2% yeast extract as the nitrogen source under the optimum growth conditions of 30°C with medium pH 6.5 at 150 rpm.

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Section: Optimisation Of Agitation Speed On Xylanase Production By Asmentioning

confidence: 99%

Bioprocessing of Agricultural Wastes as Optimised Carbon Source and Optimisation of Growth Conditions for Xylanase Production by Aspergillus brasiliensis in Agitated Solid State Fermentation (Ssf)

Lau²

2014

J Biodivers Biopros Dev

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Microbial Cell Factories for Nitrilase Production and Its Applications

Thakur¹,

Kumar

Bhatia

2023

Microbial Bioreactors for Industrial Molecules

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Optimization of arylacetonitrilase production from Alcaligenes sp. MTCC 10675 and its application in mandelic acid synthesis

Bhatia

Mehta

Bhatia

et al. 2013

Appl Microbiol Biotechnol

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Alcaligenes sp. MTCC 10675 has been isolated from soil sample using enrichment method and has nitrilase catalytic system which is highly specific for the hydrolysis of arylaliphatic nitriles. Optimization of culture conditions using response surface methodology and inducer-mediated approach enhanced arylacetonitrilase production significantly (2.4-fold). Isobutyronitrile acted as an effective inducer for the induction of arylacetonitrilase, and it is highly specific for arylacetonitriles (phenyl acetonitrile and mandelonitrile). Arylacetonitrilase has no effect on its relative velocity (V r) up to 20 mM substrate (mandelonitrile) concentration and at 30 mM mandelonitrile, 23.4 % degree of inhibition (I d) was recorded. Half life of arylacetonitrilase of Alcaligenes sp. MTCC 10675 was 27.5 h at 25 °C. Hg(2+), Ag(+), Pb(3+), and Co(2+) were strong inhibitor of arylacetonitrilase activity which resulted into 100 %, 91 %, 84 %, and 83 % inhibition, respectively. Polar protic solvent (dichloromethane, dimethylsulphooxide, and n-butanol) reduce arylacetonitrilase activity up to 80-94 % at 10 % concentration. Alcaligenes sp. MTCC 10675 has higher biocatalytic activity, i.e., 3.9 gg(-1) dcw, which is highest in comparison to till reported organism. Arylacetonitrilase-mediated hydrolysis of racemic mandelonitrile resulted into R-(-) mandelic acid with 99.0 % enantiomeric excess (e.e.).

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Production of Nitrilase by a Recombinant Escherichia coli in a Laboratory Scale Bioreactor

Cited by 4 publications

References 22 publications

Bioprocessing of Agricultural Wastes as Optimised Carbon Source and Optimisation of Growth Conditions for Xylanase Production by Aspergillus brasiliensis in Agitated Solid State Fermentation (Ssf)

Bioprocessing of Agricultural Wastes as Optimised Carbon Source and Optimisation of Growth Conditions for Xylanase Production by Aspergillus brasiliensis in Agitated Solid State Fermentation (Ssf)

Microbial Cell Factories for Nitrilase Production and Its Applications

Optimization of arylacetonitrilase production from Alcaligenes sp. MTCC 10675 and its application in mandelic acid synthesis

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