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L-Glutaminase, a therapeutically and industrially important enzyme, was produced from marine Vibrio costicola by a novel solid state fermentation process using polystyrene beads as inert support. The new fermentation system offered several advantages over the conventional systems, such as the yield of leachate with minimum viscosity and high specif...
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... Glutaminases are produced by a variety of microorganisms, including Aeromonas veronii [5], Alcaligenes faecalis [6], Aspergillus flavus [7], A. niger [8], A. oryzae [9], Bacillus subtilis [10], B. pasteurii Trends Sci. 2023; 20(4): 6504 2 of 11 [11], Clostridium welchii [12], Escherichia coli [13], Halomonas meridiana [14], Micrococcus luteus [15], Lactobacillus rhamnosus [16], Pseudomonas stutzeri [17], Rhizobium etli [18], Streptomyces canarius [19], Vibrio costicola [20], and Zygosaccharomyces rouxii [6], were isolated and well-studied. As expected, the glutaminases of these microorganisms differ in their biochemical and physicochemical properties Microorganisms are regarded as an essential source of glutaminase since the vast majority of glutaminases sold in commercial settings are derived from bacteria. ...
... Similar effects of pH on the synthesis of L-glutaminase in Hypocrea jecorina were reported to be 8.0 [1]. The optimal pH range for L-glutaminase from Vibrio sp., and Aspergillus sp. was reported to be between 7.0 and 8.5 [15,20]. ...
From Thai fermented fish sauce (Nam-pla), 59 bacterial isolates of halophilic glutaminase-producing bacteria were isolated. The hydrolysis of glutamine served as the primary screening procedure. It was discovered that strain FF5302 was an influential producer of the extracellular halophilic glutaminase enzyme. The moderately halophilic bacterium Tetragenoccus muriaticus FF5302 was identified through sequence analysis of the 16S rRNA gene, phylogenetic tree analysis, and phenotypic identification before it was possible to determine the optimal nutritional and culture conditions for its halophilic glutaminase activity. The purpose of this research was to determine the optimal nutritional and cultural conditions for producing halophilic glutaminase activity in a stirred tank bioreactor with a volume capacity of 3 L. The production of halophilic glutaminase from strain FF5302 was investigated by optimizing various physicochemical parameters. Seven potential factors are generally considered in halophilic glutaminase production, namely NaCl concentration, initial pH, temperature, incubation time, nitrogen sources, carbon sources, and inoculum size. According to the findings, the amount of halophilic glutaminase in the inoculum had an effect on the growth and activity of the enzyme when it was present at a concentration of 5 % (v/v). It was also found that halophilic glutaminase showed the highest activity (87.4 U mL−1) of strain FF5302 in SGC liquid medium containing NaCl 20 % (w/v), pH 8.0, agitation at 200 rpm, and an aeration rate of 0.05 VVM at 37 °C for 120 h. The size of the inoculum influenced both the proliferation and activity of halophilic glutaminase in the inoculum. Consequently, T. muriaticus FF5302 possessed an exceptional capacity to synthesize halophilic glutaminase. Furthermore, the halophilic glutaminase enzyme from halophilic bacteria is a prospective option for usage in the food industry as an aroma and flavor enhancer. HIGHLIGHTS muriaticus FF5302 was exceptionally capable of producing halophilic glutaminase. In addition, the enzyme is a viable candidate for usage in the food industry as an aroma and flavor enhancer. Furthermore, this study could also be helpful and valuable in improving enzyme productivity at the bioreactor scale for various industrial applications. GRAPHICAL ABSTRACT
... L-glutaminase secretion sourced from the microbial system is categorized as extracellular and intracellular both in a majority of the cases the extracellular secretion (Pandian et al. 2014;Sathish et al. 2018;Ramli et al. 2020) has been recorded in the case of marine habitats whereas in few cases the intracellular secretion has been described (Wakayama et al. 2005). The microbial systems are extremely versatile and well adapted towards elevated temperatures as it has been observed in cases Bacillus cereus Strain LC13; Alcaligenes faecalis KLU102; Vibrio azureus strain JK-79, Bacillus subtilis JK-79; Kosakonia radicincitans the temperature range lies between (30-40°C) (Kiruthika et al. 2018;More et al. 2018;Ramli et al. 2020) whereas few reports of Micrococcus luteus, Vibrio costicola, and similarly for Stenotrophomonas maltophilia it ranges between (40-60°C) (Moriguchi et al. 1994;Prabhu and Chandrasekaran 1999;Wakayama et al. 2005). Additionally, the pH is proven to play a crucial role and had a noteworthy effect on L-glutaminase biosynthesis; in the case of marine bacterial system, the pH range varies from 6.5 to 9.0; this shows the diverseness amongst the marine bacterial system and raised possible applications in the medical field as an antitumor agent. ...
In the current scenario, considerable attention is being given to the enzyme L-glutaminase (EC 3.5.1.2). It belongs to the amidohydrolase class adherent to the family of serine-reliant β-lactamases and the penicillin-binding proteins due to its higher affinity to polymerize and modify peptidoglycan synthesis. However, based on the catalytic proficiency, L-glutaminase is characterized as a proteolytic endopeptidase that cleaves peptide linkage and emancipates various byproducts, viz. ammonia along with glutamate. L-glutamine is considered the key amino acid reportedly involved in multiple metabolic pathways such as nitrogen metabolism. The present review is focused on the recent development and aspects concomitant to the biotechnological applicability of L-glutaminase predominantly from the marine habitat. Additionally, a majority of L-glutaminases finds application in cancer therapy as therapeutic agents, especially for acute lymphocytic leukaemia. The in vitro studies have been effective against various human cancer cell lines. L-glutaminase enhances the growth of probiotic bacteria. Apart from all these applications, it is suitably applicable in fermented foods as a flavour enhancer especially the umami flavour and content. Marine habitats have largely been exploited for their bio-catalytic potential but very scarcely for therapeutic enzymes. Some of the reports of such marine bacterial isolates from Bacillus sp., Pseudomonas sp. and Vibrio sp. are in the domain, but none highlights the therapeutic applications predominantly as anticancer and anti-proliferative agents.
Key points
The exploration of marine habitats along the Gujarat coasts mainly for bacteria secreting L-glutaminase is scarcely reported, and even more scarce are the amidohydrolases from these marine niches as compared to their terrestrial counterparts.
Microbial sourced amidohydrolase has wide bio-applicability that includes food, cosmetics and therapeutics especially as anticancer/anti-proliferative agent making it of immense biotechnological significance.
... The studies on L-glutaminase from Bacillus amyloliquefaciens Y-9 revealed retention of up to 68% activity of this enzyme in the presence of 20% NaCl (Mao et al. 2013). Likewise, Prabhu and Chandrasekaran (1999) reported about salt tolerance of Lglutaminase from marine Vibrio costicola; the enzyme could retain 90% of its activity in 10% NaCl solution and 75% in 15% NaCl solution (Prabhu and Chandrasekaran 1999). Another marine microbial L-glutaminase (from Pseudomonas aeruginosa CG-T8-II.1) ...
... The studies on L-glutaminase from Bacillus amyloliquefaciens Y-9 revealed retention of up to 68% activity of this enzyme in the presence of 20% NaCl (Mao et al. 2013). Likewise, Prabhu and Chandrasekaran (1999) reported about salt tolerance of Lglutaminase from marine Vibrio costicola; the enzyme could retain 90% of its activity in 10% NaCl solution and 75% in 15% NaCl solution (Prabhu and Chandrasekaran 1999). Another marine microbial L-glutaminase (from Pseudomonas aeruginosa CG-T8-II.1) ...
... Thus, a strategy that decreases blood L-glutamine levels using L-glutaminase would control the growth of cancer cells under hypoxic conditions. So far, the anticancer properties of Lglutaminase have been reported from marine bacteria (Ahmed et al. 2016;Aly et al. 2017;Orabi et al. 2020;Pandian et al. 2014;Prabhu and Chandrasekaran 1999) while no data of yeast and fungi is available in this regard. Alcaligenes faecalis KLU102, Streptomyces sp. ...
Deamination of L-glutamine to glutamic acid with the concomitant release of ammonia by the activity of L-glutaminase (L-glutamine amidohydrolase EC 3.5.1.2) is a unique reaction that also finds potential applications in different sectors ranging from therapeutics to food industry. Owing to its cost-effectiveness, rapidity, and compatibility with downstream processes, microbial production of L-glutaminase is preferred over the production by other sources. Marine microorganisms including bacteria, yeasts, and moulds have manifested remarkable capacity to produce L-glutaminase and, therefore, are considered as prospective candidates for large-scale production of this enzyme. The main focus of this article is to provide an overview of L-glutaminase producing marine microorganisms, to discuss strategies used for the lab- and large-scale production of these enzyme and to review the application of L-glutaminase from marine sources so that the future prospects can be understood.
Key points
• L-glutaminase has potential applications in different sectors ranging from therapeutics to food industry
• Marine microorganisms are considered as prospective candidates for large-scale production of L-glutaminase
• Marine microbial L-glutaminase have great potential in therapeutics and in the food industry
... Glutaminase is often used in Chinese traditional fermented foods such as soy sauce, and fermented beans, etc. Glutaminolytic enzymes are produced by many organisms like plants, animal tissues, and microorganisms, including bacteria, yeasts, and fungi. In general, glutaminases from Aeromonas veronii [2], Aspergillus flavus [3], A. niger [4], A. oryzae [5], Bacillus subtilis [6], Clostridium welchii [7], Escherichia coli [8], Pseudomonas stutzeri [9], Rhizobium etli [10], Streptomyces canarius [11], Vibrio costicola [12], and Zygosaccharomyces rouxii [13] have been isolated and well-studied. ...
The Plackett–Burman design was used to efficiently select the key cultural parameters for the production of halophilic glutaminase by moderately halophilic bacterium Tetragenococcus muriaticus FF5302. Eleven variables were selected, i.e., glutamine, peptone, yeast extract, glucose, fructose, KCl, MgSO4, NaCl, temperature, pH, and inoculum size, which were used to identify the most significant variables that affected halophilic glutaminase production in 12 experimental trials. Statistical analysis demonstrated that glutamine, pH, and temperature had the most significant effects on halophilic glutaminase production. The maximum halophilic glutaminase activity of 199.27 U ml-1 was observed after 120 h of fermentation. After Plackett-Burman design experiments, the glutaminase activity was found to be 2.28 folds increase compared to one factor at a time method. This demonstrates that testing all factors simultaneously may be a powerful and useful statistical approach for the rapid identification of production parameters.
... Summary of some enzymes from marine bacteria and fungi and their biotechnological and industrial potential use are described in table i, ii. 2,3,34,36,[39][40][41][42][43][44][45][46][47][48][49][50][51][52][53][54][55][56] Industrial applications of enzymes from marine habitat ...
Marine microorganisms are considered as a great source of biodiversity. The demand of marine enzymes is extensively and increasingly used in research and in various industries due to their diversity to survive under extreme conditions such as pH, temperature, light, atmospheric pressure, and the availability of nutrients. Despite the huge biodiversity and benefits present in marine enzymes, their biotechnology potentials remain largely unexplored. Marine enzymes can be produced and extracted from microorganisms, plants and animals using fermentation processes. Some enzymes produced by marine microorganisms have potential application in various productions such as pharmaceuticals, foods, textile, agricultural, chemical, and biomedical industries. They offer new opportunities for new line of research and future biotechnological applications. Marine microorganisms are considered as a source of enzymes with potential interest to various commercial industries and many researchers. In this mini review, an overview of enzymes was provided from marine microorganisms and their application in biotechnology.
... The sterilized solid substrate media was inoculated with 2% (v/w) inoculum size of the strain marine, B. subtilis JK-79. The contents were mixed thoroughly and incubated in a slanting position at 37°C for 24 h under 80% relative humidity (Prabhu and Chandrasekaran, 1997). ...
... This is may be because of the inactivation of the enzyme. The result is in accordance with literature reports (Prabhu and Chandrasekaran, 1997;Sabu et al., 2000;Kashyap et al., 2002). ...
... costicola (Prabhu and Chandrasekaran, 1997) and T. koningii (Sayed, 2009). ...
... Among the different substrates investigated, the enzyme showed high specificity towards its natural substrate L-asparagine, very low specificity towards L-aspartic acid, while no activity towards L-glutamine and L-glutamic acid ( Figure 6). Our findings were in concordance with that of Prabhu, Sahira and Lincoln in Vibrio costicola, Acinetobacter baumannii and Trichoderma viride respectively [28,29,20]. This property of purified enzyme increases its potential to be used in therapeutics and food industries. ...
... Our findings were in concordance with that of Prabhu, Sahira and Lincoln in Vibrio costicola, Acinetobacter baumannii and Trichoderma viride respectively. 20,28,29 This property of purified enzyme increases its potential to be used in therapeutics and food industries. ...
... Carbon source represents the energy source that will be available for growth of the microorganism, carbohydrates and related compounds are superior carbon sources for many genera of microbes (Rosalie, 1999) .Different carbon sources namely Glucose, Lactose, Sucrose, Mannitol, Sorbitol and Pectin at 1% were added to the basal medium of Burkholderia cepacia complex, the maximum enzyme production was promoted by glucose (7.87 U/ml and 3.81 U/ml for extra and intracellular glutaminase respectively) followed by mannitol (Fig.2).The enhanced production of L-glutaminase by the incorporation of glucose to the medium may be attributed to the positive influence of glucose as a co-metabolic agent for enhanced enzyme biosynthesis (Prasanna & Raju, 2012). These results were similar to those reported by production by Vibrio costicola (Prabhu & Chandrasekaran, 1999) and by Brevundimonas diminuta MTCC (Jayabalan et al, 2010) and by Beauveria sp (Sabu et al, 2000). ...
An L-glutaminase producing microorganism was isolated and identified as Burkholderia cepacia complex. The isolated microorganism produced intra and extracellular glutaminase. Maximal L-glutaminase yield (14.74 U/ml and 5.84 U/ml for extra and intracellular glutaminase respectively) were obtained in a medium supplemented with glucose, Ammonium sulphate and Sodium sulphate as the best carbon, nitrogen and mineral sources respectively. Initial pH 7.0 , at 28°C and agitation speed 150 rpm, inoculum concentration 2% after 24 h incubation period. Both physico-chemical and nutritional parameters had played a significant role in the production of the enzyme.
Aim and objective:
To review the applications and production studies of reported antileukemic drug L-glutaminase under Solid-state Fermentation (SSF).
Overview:
An amidohydrolase that gained economic importance because of its wide range of applications in the pharmaceutical industry, as well as the food industry, is L-glutaminase. The medical applications utilized it as an anti-tumor agent as well as an antiretroviral agent. L-glutaminase is employed in the food industry as an acrylamide degradation agent, as a flavor enhancer and for the synthesis of theanine. Another application includes its use in hybridoma technology as a biosensing agent. Because of its diverse applications, scientists are now focusing on enhancing the production and optimization of L-glutaminase from various sources by both Solid-state Fermentation (SSF) and submerged fermentation studies. Of both types of fermentation processes, SSF has gained importance because of its minimal cost and energy requirement. L-glutaminase can be produced by SSF from both bacteria and fungi. Single-factor studies, as well as multi-level optimization studies, were employed to enhance L-glutaminase production. It was concluded that L-glutaminase activity achieved by SSF was 1690 U/g using wheat bran and Bengal gram husk by applying feed-forward artificial neural network and genetic algorithm. The highest L-glutaminase activity achieved under SSF was 3300 U/gds from Bacillus sp., by mixture design. Purification and kinetics studies were also reported to find the molecular weight as well as the stability of L-glutaminase.
Conclusion:
The current review is focused on the production of L-glutaminase by SSF from both bacteria and fungi. It was concluded from reported literature that optimization studies enhanced L-glutaminase production. Researchers have also confirmed antileukemic and anti-tumor properties of the purified L-glutaminase on various cell lines.
