Occurrence of Streptomyces aurantiacus in mangroves of Bhitarkanika

Gupta, Nibha; Mishra, Smruti Ranjan; Basak, Uday Chand

doi:10.21161/mjm.00807

Cited by 21 publications

(17 citation statements)

References 1 publication

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“…In the present study, among the five sites studied, pH of Budhabalanga was maximum (8.45 ± 0.09) is alkaline in comparison to Devi having minimum (5.79 ± 0.14) is acidic in nature which is consistent with the range (4.5 to 9) specified by Costerton et al [15] for microbial activity to take place whereas in contrast more uptake of CO 2 by the photosynthetic organisms could have increased the pH level. Similar range of pH has also been reported by earlier workers [16][17][18]. A significant correlation obtained between for pH with salinity, alkalinity and conductivity (Tables 2-6) has revealed the influence of salinity over pH.…”

Section: Discussionsupporting

confidence: 89%

Physico-Chemical Sediment Properties of Mangroves of Odisha, India

Sahoo¹,

Jee²,

Dhal³

et al. 2017

J Oceanogr Mar Res

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Section: Discussionsupporting

confidence: 89%

Physico-Chemical Sediment Properties of Mangroves of Odisha, India

Sahoo¹,

Jee²,

Dhal³

et al. 2017

J Oceanogr Mar Res

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“…Several terrestrial Streptomyces are capable of producing detectable amounts of L-asparaginase. There are limited reports on production of L-asparaginase from marine Streptomyces like Streptomyces aurantiacus (Gupta et al, 2007). Streptomycetes and Micromonospora sp are distributed in both marine and terrestrial environments.…”

Section: Resultsmentioning

confidence: 99%

Comparative Studies on Effect of Carbon and Nitrogen Sources on L -Asparaginase Production

Raja¹,

A²,

Salique³

et al. 2017

Int J Appl Sci Biotechnol

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Marine actinomycetes sediment samples were collected from Gulf of Mannar costal region, Kayalpatinam, located at Tuticorin district, Tamilnadu, India. Marine actinomycetes were isolated and evaluated for activity of L-asparaginase production. A total of 10 marine actinomycetes strains were isolated. Among 10 isolates, six were belongs to Streptomyces sp, three were belongs to Micromonospora sp and one was to Micropolyspora sp. Based on phenotypic characteristics, actinomycetes strains were screened for L-asparaginase production. Streptomyces sp KPMS5 and Micromonospora sp KPMS10 were showed large pink coloration on L-asparaginase production medium. The strains were further studied for maximum production and characterizations of culture condition of L-asparaginase enzyme were evaluated. Effect of substrate on L-asparaginase production was evaluated by enzyme assy. Maximum enzyme assay (1.4 mM) was observed on glucose followed by starch (1.12Mm) by Micromonospora sp KPMS10. In Streptomyces sp KPMS5 showed maximum of 1.25mM of enzyme assay on glucose substrate followed by lactose 1.17mM. Yeast extract was effectively used as substrate for maximum production of L-asparaginase by submerged fermentation. Further studies on purification and characterization are required to support the application of enzyme. The finding concludes isolates belongs to non-Streptomyces sp like Micromonospora sp is a potential novel source for L-asparaginase production.

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“…Recently, Gupta et al [5] reported that marine actinomycetes have been shown to be a good source for L-Asparaginase because of extreme adaptation with in marine environment.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Purification of High Efficiency L-asparaginase by Quantitative Preparative Continuous-elution SDS PAGE Electrophoresis

M¹,

Selvam²

2011

J Microbial Biochem Technol

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An Unique extracelluar glutaminase free L-asparaginase from novel marine Actinomycetes was isolated to perceptible homogeneity in agro industrial wastes. Quantitative Preparative Continuous-Elution SDS PAGE Electrophoresis is a high-resolution method for the preparative isolation of L-Asparaginase in biological samples. The enzyme was purified 248.68-fold and showed a final specific activity of 5035.28 IU/mg with an 80.71% yield. The homotetramer enzyme has a molecular mass of 133.25 kDa and an isoelectric point of approximately 5.4.Kinetic parameters, Km and Vmax of purified L-asparaginase from Streptomyces radiopugnans MS1 were found to be 0.0598, 3.5478 IU µg -1 respectively. The de novo sequencing strategy presented here provides a rapid and reliable means to identify proteins in Streptomyces radiopugnans MS1. The purified L-asparaginase has no glutaminase activity, which can diminish the leeway of side effects during the itinerary of anti-malignancy therapy.

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Occurrence of Streptomyces aurantiacus in mangroves of Bhitarkanika

Cited by 21 publications

References 1 publication

Physico-Chemical Sediment Properties of Mangroves of Odisha, India

Physico-Chemical Sediment Properties of Mangroves of Odisha, India

Comparative Studies on Effect of Carbon and Nitrogen Sources on L -Asparaginase Production

Isolation and Purification of High Efficiency L-asparaginase by Quantitative Preparative Continuous-elution SDS PAGE Electrophoresis

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