Asparaginase and Glutaminase Activities of Micro-organisms

Abstract

S U M M A R YL-Asparaginase and L-glutaminase activities were detected in many microorganisms and the distribution of these activities was found to be related to the classification of micro-organisms.Among 464 bacteria, the activities occurred in many Gram-negative bacteria and in a few Gram-positive bacteria. Most members of the family Enterobacteriaceae possessed L-asparaginase. L-Asparaginase and L-glutaminase occurred together in a large proportion of pseudomonads. Among Gram-positive bacteria many strains of Bacillus pumilus showed strong L-asparaginase activity. Amidase activities were also observed in several strains in other families.L-Asparaginase activity was not detected in culture filtrates of 261 strains of species of the genera Streptomyces and Nocardia, but L-asparaginase and Lglutaminase were detected when these organisms were sonicated.The amidase activities in culture filtrates of 4158 fungal strains were tested. All the strains of Fusarium species formed L-asparaginase. Organisms of the genera Hjyomyces and Nectria, which are regarded as the perfect stage of the genus Fusarium, also formed L-asparaginase. Several Penicillium species formed L-asparaginase. Two organisms of the family Moniliaceae formed L-glutaminase together with L-asparaginase, and a few ascomycetous fungi formed L-asparaginase or L-glutaminase.Among I 326 yeasts, L-asparaginase or L-glutaminase occurred frequently in certain serological groups of yeasts : VI (Hansenula) group, Cryptococcus group and Rhodotorula group. Many strains of Sporobolomyces species also showed L-asparaginase activity. Several strains of Cryptococcus and Rhodotorula group possessed L-glutaminase and L-asparaginase. L-Glutaminase alone was formed in many strains of Candida scottii and Cryptococcus albidus, both of which are related to Basidiomycetes.

Production of Extracellular Anti-leukemic Enzyme L-asparaginase from Fusarium solani AUMC 8615 Grown under Solid-State Fermentation conditions: Purification and Characterization of The Free and Immobilized Enzyme

“…The change of the indicator color from yellow to pink resulted from the increase in pH due to ammonia release. The ammonia along with L-aspartic acid is formed by the deamination reaction of the substrate L-asparagine by L-asparaginase (Imada et al, 1973 andGulati et al, 1997). Thus, the potential strain was selected on the basis of the appearance of a pink zone around the fungal colonies as well as growth of the organism.…”

“…L-asparaginase Assay L-asparaginase activity was measured following the method of Imada et al (1973). This method utilizes the determination of ammonia liberated from Lasparagine in the enzyme reaction by the Nessler's reaction.…”

L-glutaminase production by Trichoderma koningii under solid-state fermentation

“…L-glutaminase was assayed by direct Nesslerization according to Imada et al [13]. The enzymatic reaction mixture contains 1 ml of 1% L-glutamine in citrate-phosphate buffer (pH 7.0) and 1ml of the crude enzyme incubated at 30°C for 1 h. The enzymatic acitivty was stopped by adding 0.5 ml of 1.5 M trichloroacetic acid.…”

“…L-glutaminase production by various bacterial genera under submerged culture conditions was extensively studied [12][13][14]. Furthermore, submerged cultures of Verticillium malthousei [13], Aspergillus sojae [15], A. nidulans [16], Tilachlidium humicola [17] and Penicillium notatum [18] had been used for L-glutaminases production. It appears from the documented literature a few reports being intensive, only, on the production of L-glutaminase by Aspergillus oryzae [19], Beauveria sp.…”

Microbial Amidases and their Industrial Applications: A Review

“…A large proportion of strains of Pseudomonas species showed L-asparaginase and L-glutaminase simultaneously. Most members of the Enterobacteriaceae are active for L-asparaginase but not so active for L-glutaminase [33]. While Roberts et al [21] isolated Achromobacteraceae from the soil samples and observed that this family has L-glutaminase and L-asparaginase activity in a ratio of 1.2:1.…”