Continuous production of l-glutaminase by an immobilized marine Pseudomonas sp BTMS-51 in a packed bed reactor

Kumar, Subhash; Chandrasekaran, M.

doi:10.1016/s0032-9592(03)00035-9

Cited by 48 publications

(19 citation statements)

References 15 publications

(10 reference statements)

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“…In the case of fungi both intra and extracellular glutaminase from Aspergillus oryzae were inhibited by Hg, Cr and Fe but were not affected by sulphydroxyl reagents. EDTA, Na 2 SO 4 , and p-c Woromercuribenzoate strongly inhibited the Micrococcus luteus glutaminase I while glutaminase II was inhibited by EDTA, HgCh, Na 2 SO 4 , CuCh and FeCh 39 .…”

Section: Effect Of Various Substances and Heavy Metalsmentioning

confidence: 91%

“…However, it was reported that addition of glucose enhanced the enzyme production in C. nodaensis 38 , Pseudomonas sp. 39 , Streptomyces rimosus 40 , Providencia sp. 41 , T. koningii 42 and Beauveria sp.…”

Section: Effect Of Additional Carbon and Nitrogen Sources On L-glutammentioning

confidence: 99%

“…One of the most promising therapeutic applications ever proposed for L-Glutaminase is in the treatment of HIV 39 . Roberts et al have patented a therapy for HIV, where L-Glutaminase from Pseudomonas sp.…”

Section: Effect Of Various Substances and Heavy Metalsmentioning

confidence: 99%

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Untitled

2014

IJPSR

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ABSTRACT:One of the prime candidates in the treatment of debilitating human cancers includes a family of enzymes referred to as L-glutaminases. The antitumor activity of these enzymes found effective in countering Acute Lymphoblastic Leukemia (ALL a commonly diagnosed pediatric cancer.). .Apart from therapeutic use, it is having a number of other applications like in food industry, analysis and in production of fine chemicals. This review, hence, mainly focuses on the biochemical aspects of L-Glutaminase production, aiming to comprehend the physiochemical characteristics, application of LGlutaminase and its properties. Processes central to these biochemical aspects, including submerged fermentation and Solid state fermentation of Lglutaminase producing organisms are also discussed.

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Section: Effect Of Various Substances and Heavy Metalsmentioning

confidence: 91%

Section: Effect Of Additional Carbon and Nitrogen Sources On L-glutammentioning

confidence: 99%

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2014

IJPSR

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“…A glutaminaseasparaginase enzyme from Achromobacter has shown anti leukemic effects in patients with acute lymphoblastic leukemia and acute myelois leukemia in a preliminary clinical trial [65]. Moreover, one of the most promising therapeutic applications ever proposed for the L-glutaminase is in treatment of HIV [66].…”

Section: Applications Of Microbial Amidases Therapeutic Applicationsmentioning

confidence: 99%

Microbial Amidases and their Industrial Applications: A Review

El-Ghonemy¹

2015

J Med Microb Diagn

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Among the pediatric cancer in developed countries, acute leukemia ¬constitutes the major part with affecting 30-45 per 1,000,000 children each year. The effect of treatment varies with differences in patients clinical, immunologic and genetic characteristics. Therefore, the search for efficient drugs to solve this problem is being continued worldwide. Although several kinds of treatments are available, enzyme therapy is equally effective. Enzymes have been used as drugs; likewise L-asparaginase and L-glutaminase had received much attention in recent years due to their anticarcinogenic potential. These enzymes constitute one of the most biotechnologically and biomedically important group of therapeutic enzymes accounting for about 40% of the total worldwide enzyme sales. Various sources are found to be good producers of the enzymes: bacteria, fungi along with some of the plant and animal species. Food and Drug Administration and World Health Organization have approved L-asparaginase for the effective treatment of acute lymphoblastic leukemia and lymphsarcoma. L-asparaginase and L-glutaminase break down L-asparagine or L-glutamine into L-aspartic acid or L-glutamic acid, respectively, and ammonia. L-asparagine depletion results in nutritional deprivation, inhibition of protein synthesis, and subsequent apoptotic cell death in lymphoblasts. On the other hand, the ability of L-asparaginase to selectively hydrolyzes L-asparagine into L-aspartateis a potential way to reduce the amount of free L-asparagine in the starting materials of food production, thus reducing the imminent risk of generating a potential carcinogenic and neurotoxic acrylamide that formed from L-asparagine and reducing sugars in carbohydrate-containing foods (such as snacks and biscuits) when they are heated above 120oC. Therefore, the present review is an attempt to compile information on the sources, antino plastic action and industrial application of microbial amidases enzymes.

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“…In recent years, L-glutaminase has received attention as a therapeutic agent against cancer and HIV (Roberts et al, 1970;Chandrasekaran et al, 1991;Kumar and Chandrasekaran, 2003), as a bio-sensing agent in monitoring glutamine levels (Kashyap et al, 2002;Zhao et al, 2004), for the production of specialty chemicals like theanine by c-glutamyl transfer reactions and as a flavour enhancer in the food industry (Sivakumar et al, 2006). The use of L-glutaminase as a flavour-enhancing agent in Chinese foods has replaced the use of monosodium glutamate which acts as an allergen for individuals (Rohde et al, 1996;Masuoa et al, 2004;Thongsanit et al, 2008;Jeon et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Optimised production of L-glutaminase: A tumour inhibitor from Aspergillus flavus cultured on agroindustrial residues

Nathiya¹,

Nath²,

Angayarkanni³

et al. 2011

Afr. J. Biotechnol.

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L-Glutaminase, an amidohydrolase enzyme has been a choice of interest in the treatment of lymphoblastic leukemia. This study investigates the production and optimization of extracellular glutaminase enzyme using several agro-industrial residues by Aspergillus flavus KUGF009 using SSF (solid state fermentation). Effect of process variables namely substrates, incubation period, temperature, moisture content, initial pH, supplementary carbon and nitrogen sources and metal ions on the production of L-glutaminase was studied and accordingly, optimum conditions were determined. A. flavus KUGF009 was cultured in tea dust to produce L-glutaminase. The organism produced high levels of glutaminase under optimized culture conditions on the 5th day of incubation at an optimum pH 4.0, temperature 30°C and moisture content 50% by SSF. Enhanced production occurred on the addition of dextrose, yeast extract and MgSO 4 as nutritional factors.

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Continuous production of l-glutaminase by an immobilized marine Pseudomonas sp BTMS-51 in a packed bed reactor

Cited by 48 publications

References 15 publications

Untitled

Untitled

Microbial Amidases and their Industrial Applications: A Review

Optimised production of L-glutaminase: A tumour inhibitor from Aspergillus flavus cultured on agroindustrial residues

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