Microbial glutaminase: biochemistry, molecular approaches and applications in the food industry

Nandakumar, Renu; Yoshimune, Kazuaki; Wakayama, Mamoru; Moriguchi, Mitsuaki

doi:10.1016/s1381-1177(03)00075-4

Cited by 122 publications

(86 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5). L-glutaminase with molecular mass of 132 and 137 kDa was reported from Acinetobacter glutaminasificans and Pseudomonas aeruginosa respectively (Nandakumar et al, 2003).…”

Section: Resultsmentioning

confidence: 99%

“…The activity of glutaminase, which is responsible for the synthesis of glutamic acid, makes it an important additive during soy sauce fermentation. Attempts to increase the glutamate content of soysuace using a salt tolerant and thermo tolerant glutaminases have drawn much attention (Nandakumar et al, 2003). Commercial importance demands not only the search for new and better yielding microbial strains, but also economically viable bioprocesses for its large scale production.…”

Section: Introductionmentioning

confidence: 99%

“…Previous reports state that B. diminuta TPU 5720 produces an amidase acting L-stereoselectively on phenylalaninamide (Komeda et al, 2006). It has been identified that approximately 60 microbial species could produce L-glutaminase (Nandakumar et al, 2003). Until now there are no reports available for the presence of L-glutaminase from B. diminuta.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Extracellular L-Glutaminase Production By Marine Brevundimonas Diminuta MTCC 8486

Jayabalan¹,

Jeeva²,

Inbakandan³

et al. 2010

Int. Jour. Appl. Bio-Eng.

View full text Add to dashboard Cite

show abstract

“…5). L-glutaminase with molecular mass of 132 and 137 kDa was reported from Acinetobacter glutaminasificans and Pseudomonas aeruginosa respectively (Nandakumar et al, 2003).…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Extracellular L-Glutaminase Production By Marine Brevundimonas Diminuta MTCC 8486

Jayabalan¹,

Jeeva²,

Inbakandan³

et al. 2010

Int. Jour. Appl. Bio-Eng.

View full text Add to dashboard Cite

show abstract

“…Amidases are widely distributed in plants, animals, rodents and microorganisms including bacteria, fungi, actinomycetes [24][25][26]. However, the inability of the plant and animal amidases to meet current world demands has led to an increased interest in microorganisms which represent an excellent source of enzymes [8].…”

Section: Occurrence and Distributionmentioning

confidence: 99%

Microbial Amidases and their Industrial Applications: A Review

El-Ghonemy¹

2015

J Med Microb Diagn

View full text Add to dashboard Cite

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.

show abstract

“…Besides its applications in cancer therapy, Lglutaminase is also a much sought-after enzyme in the food industries as a flavour-enhancing agent (Nandakumar et al 2003), for the production of acrylamide-free potato food (Pedreschi et al 2008), and as a biosensor that detects glutamine (Padma et al 2010). Previous studies have shown that marine environments could be a source of many enzymes that display useful characteristics, including salt tolerance and stability under various conditions (Chandrasekaran et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Optimization and purification of anticancer enzyme L-glutaminase from Alcaligenes faecalis KLU102

et al. 2014

View full text Add to dashboard Cite

L-Glutaminase, an amidohydrolase, is gaining importance on account of its potential anticancer activity. L-Glutaminase produced by Alcaligenes faecalis KLU102, isolated from the marine realm (Bay of Bengal), exhibits potential anticancer activity. Response surface methodology was employed for optimizing the medium composition. The concentrations of the various constituents were as follows: arabinose (2%), skim milk (4%), and salts viz. K2HPO4, KH2PO4, MgSO4, and NaCl (2%). The bacterium grown in the optimized medium yielded an enzyme activity of 1.34 ± 0.07 IU/mg in shake-flask cultures and this doubled (2.77 ± 0.35 IU/mg) when scale-up studies were conducted using a 3-L fermenter. The enzyme was purified to homogeneity using ion-exchange chromatography, and the purified enzyme was found to have a specific activity of 54.72 IU/mg, with a molecular weight of 37 kDa. Immobilization of the enzyme on PEG-PHB nanoparticles improved the stability of the enzyme significantly. Purified L-glutaminase exhibited cytotoxic activity against HeLa cells, as assayed by the MTT assay, with an IC50 value of 12.5 µg/mL.

show abstract

Microbial glutaminase: biochemistry, molecular approaches and applications in the food industry

Cited by 122 publications

References 53 publications

Extracellular L-Glutaminase Production By Marine Brevundimonas Diminuta MTCC 8486

Extracellular L-Glutaminase Production By Marine Brevundimonas Diminuta MTCC 8486

Microbial Amidases and their Industrial Applications: A Review

Optimization and purification of anticancer enzyme L-glutaminase from Alcaligenes faecalis KLU102

Contact Info

Product

Resources

About