2013
DOI: 10.1016/s2221-1691(13)60182-3
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Screening and characterization of extracelluar L-asparaginase producing Bacillus subtilis strain hswx88, isolated from Taptapani hotspring of Odisha, India

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Cited by 43 publications
(24 citation statements)
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References 14 publications
(41 reference statements)
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“…When L-asparaginase is administered to a system, it discontinues asparagine supply to tumor cells causing its enzymatic cleavage into L-aspartate and ammonia. Eventually, starvation for L-asparagine disturbs the metabolic status of these malignant cells, thereby leading them to apoptotic death (Pradhan et al, 2013). Apart from its antileukemic activity, L-asparaginase has other applications in the food industries as an agent for producing acrylamidefree food products (Ciesarova et al, 2006), and also for constructing a diagnostic biosensor (Erdogan et al, 2014).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…When L-asparaginase is administered to a system, it discontinues asparagine supply to tumor cells causing its enzymatic cleavage into L-aspartate and ammonia. Eventually, starvation for L-asparagine disturbs the metabolic status of these malignant cells, thereby leading them to apoptotic death (Pradhan et al, 2013). Apart from its antileukemic activity, L-asparaginase has other applications in the food industries as an agent for producing acrylamidefree food products (Ciesarova et al, 2006), and also for constructing a diagnostic biosensor (Erdogan et al, 2014).…”
Section: Introductionmentioning
confidence: 99%
“…The enzyme has been reportedly isolated from various bacterial origins such as Bacillus subtilis (Pradhan et al, 2013), Bacillus aryabhattai (Singh et al, 2013), Escherichia (Warangkar and Khobragade, 2010), Xanthomonas, Pectobacterium, Photobacterium (Abbas et al, 2010), Aerobacter, Erwinia, Serratia, Streptomyces (Agarwal et al, 2011), and Corynebacterium (Mesas et al, 1990) species; and from fungal origins such as Aspergillus and Candida species (Kumar and Sobha, 2012); and a few from protozoa, for example, Tetrahymena pyriformis (Triantafillou et al, 1988). Though the enzyme is widely distributed, only some of these L-asparaginases possess antineoplastic activity and among the microbial sources, the most commercially notable ones are Escherichia coli, Erwinia carotovora and Serratia marcescens (Kumar and Shobha, 2012).…”
Section: Introductionmentioning
confidence: 99%
“…Due to broad diversity, easy to production, recovery and especially its susceptibility towards genetic manipulation for higher production of enzymes, microbes was found to be best alternative for L-asparaginase production. Numerous bacterial species viz., Escherichia (Warangkar et al, 2010), Aerobacter, Erwinia, Serratia (Agarwal et al, 2011), Xanthomonas (Abbas et al, 2010), Bacillus was reported to produce L-asparaginase (Pradhan et al, 2013;Sunitha et al, 2010;Thenmozhi et al, 2011). The present investigation carried out with isolation and screening of L-asparaginase producing bacteria from diversified soil samples, fermentation studies, partial purification of Lasparaginase from potential isolates and preliminary microbial characterization of the isolates.…”
Section: Issn: 2319-7706 Volume 6 Number 9 (2017) Pp 784-792mentioning
confidence: 89%
“…They widely exist in all living organisms, including microorganisms, plants and animals but due to its tedious extraction procedure, microorganisms have been found to be more efficient and cost effective Hendriksen et al, (2009). The selection and production of extracellular asparaginase be preferred over other intracellular enzyme because of having easy extraction, protease deficient compartment and relatively free from endotoxins which affect in minimization of adverse effects (Pradhan et al, 2013) Each bacterial species has its own particular nutritional and environmental requirement and there is no standard medium has been developed for the optimum production of asparaginase from bacterial species (Chidambaram et al, 2009). …”
Section: Introductionmentioning
confidence: 99%