Studies on efficient production of a novel l-asparaginase by a newly isolated IGS-131 and its heterologous expression in .

Mihooliya, Kanti N and Nandal, Jitender and Kumari, Alka and Nanda, Sidhanta and Verma, Himanshu and Sahoo, Debendra K (2020) Studies on efficient production of a novel l-asparaginase by a newly isolated IGS-131 and its heterologous expression in . 3 Biotech, 10 (4). p. 148. ISSN 2190-572X

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Abstract

In the current study, the production of novel glutaminase free l-asparaginase from a new microbial source ( IGS-131) is reported. Optimization of l-asparaginase production using conventional and statistical optimization techniques resulted in an enzyme yield of 37.63 IU/mL, which was 3.45-fold higher than the initial enzyme activity (i.e., 10.91 IU/mL). l-Asparaginase production from . IGS-131 was successfully carried out at the bioreactor level and investigations on the effect of agitation rates showed a maximum asparaginase yield of 38.88 IU/mL after 24 h fermentation at 400 rpm. The l-asparaginase gene from this source, showing 78% identity with a reported sequence in GenBank, was expressed in rosetta DE3. The molecular weight of the recombinant protein was determined as 35.6 kDa. Downstream processing of recombinant l-asparaginase resulted in a purified protein concentration of 62.53 mg/L, which showed good free radical scavenging activity of 62%. The current findings provide promising results for a process of l-asparaginase production from . IGS-131. Furthermore, the recombinant production of this enzyme could help in avoiding the complexity of down streaming processes associated with the purification of this enzyme from wild-type organisms.

Item Type: Article
Additional Information: Copyright of this article belongs to Springer.
Uncontrolled Keywords: Antioxidant; Bioreactor; Pseudomonas resinovorans; Response surface methodology; l-Asparaginase
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 04 Apr 2020 17:13
Last Modified: 04 Apr 2020 17:13
URI: http://crdd.osdd.net/open/id/eprint/2550

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