Enhanced lipase production by mutation induced Aspergillus japonicus

Karanam, Sita Kumari; Medicherla, Narasimha Rao

doi:10.5897/ajb2008.000-5054

Cited by 28 publications

(10 citation statements)

References 7 publications

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“…In this work, the production of extracellular lipase by A. japonicus using olive oil as substrate was evaluated, and the obtained enzymatic extract clearly demonstrate the ability of microorganism to hydrolyze triacylglycerols, achieving, 20.42 U ml −1 and 934.958 U mg −1 of lipase hydrolytic activity and specific activity, respectively. These results are in accordance with those (20.6 U ml −1 ) obtained by Karanam et al [44] in the hydrolysis of p-nitrophenyl palmitate (pNPP) by a lipase preparation using a genetically modified strain of A. japonicus MTCC 1975. Evaluating the lipase production by A. japonicus LAB01 in medium supplemented with sunflower oil (1% w w −1 ), at pH 6.0, Souza et al [47] achieved 28.04 U ml −1 on pNPP hydrolysis.…”

Section: Production Of Lipase By a Japonicussupporting

confidence: 92%

“…As aforementioned, microbial lipases, cf., Aspergillus-based lipases present great potential to be used in many industrial fields, to produce detergents, biodiesel, bread, functional foods, among others [43]. There are few reports about the microbial production of lipase by A. japonicus in the literature [44][45][46][47][48][49][50]. However, among the works found, it is clear that the kinetic parameters (K M and V max ) are directly affected by the composition of nutritional media, substrate used in the enzymatic assay, type of cultivation (solid or submerged) and several processual parameters, i.e., pH, temperature and agitation [44][45][46][47][48][49][50].…”

Section: Production Of Lipase By a Japonicusmentioning

confidence: 99%

“…There are few reports about the microbial production of lipase by A. japonicus in the literature [44][45][46][47][48][49][50]. However, among the works found, it is clear that the kinetic parameters (K M and V max ) are directly affected by the composition of nutritional media, substrate used in the enzymatic assay, type of cultivation (solid or submerged) and several processual parameters, i.e., pH, temperature and agitation [44][45][46][47][48][49][50]. The ideal temperature to achieve high lipase production yields generally ranges from 30 to 50 • C [45][46][47][48][49][50] and pH 6.0 to 8.5 which are considered optimal for A. japonicus growth and therefore the successful production of lipase [45][46][47][48][49][50].…”

Section: Production Of Lipase By a Japonicusmentioning

confidence: 99%

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Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

et al. 2021

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Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that presented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50 °C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.

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Section: Production Of Lipase By a Japonicussupporting

confidence: 92%

Section: Production Of Lipase By a Japonicusmentioning

confidence: 99%

Section: Production Of Lipase By a Japonicusmentioning

confidence: 99%

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Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

et al. 2021

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“…Random mutagenesis has been applied in a large number of fungal species for many industrial purposes, such as improved cellulase production in Aspergillus sp. [35], lipase production by Aspergillus japonicus [26] or citric acid overproduction by the industrial workhorse Aspergillus niger [36]. Moreover, UV-derived mutations were reported in A. niger to increase Filter Paper activity (FPase) and carboxymethyl cellulase (CMCase) production [37].…”

Section: Physical and Chemical Mutagenesismentioning

confidence: 99%

Strategies for the Development of Industrial Fungal Producing Strains

Salazar-Cerezo

Vries

Garrigues

2023

JoF

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The use of microorganisms in industry has enabled the (over)production of various compounds (e.g., primary and secondary metabolites, proteins and enzymes) that are relevant for the production of antibiotics, food, beverages, cosmetics, chemicals and biofuels, among others. Industrial strains are commonly obtained by conventional (non-GMO) strain improvement strategies and random screening and selection. However, recombinant DNA technology has made it possible to improve microbial strains by adding, deleting or modifying specific genes. Techniques such as genetic engineering and genome editing are contributing to the development of industrial production strains. Nevertheless, there is still significant room for further strain improvement. In this review, we will focus on classical and recent methods, tools and technologies used for the development of fungal production strains with the potential to be applied at an industrial scale. Additionally, the use of functional genomics, transcriptomics, proteomics and metabolomics together with the implementation of genetic manipulation techniques and expression tools will be discussed.

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“…Classically, enzyme production by microorganisms has been enhanced by random mutagenesis, including mutants induced by chemicals such as N-methyl-N=-nitro-N-nitrosoguanidine (NTG) and ethyl methanesulfonate (EMS) and by UV radiation (5,6). Strain improvement processes have been described for producing various industrial enzymes, including lipases, chitinases, cellulases, glucoamylases, and proteases (7)(8)(9)(10)(11)(12). Enzymes for industrial use are produced by growing bacteria and fungi under submerged or solid-state conditions.…”

mentioning

confidence: 99%

Combined Drug Resistance Mutations Substantially Enhance Enzyme Production in Paenibacillus agaridevorans

et al. 2018

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This study shows that sequential introduction of drug resistance mutations substantially increased enzyme production in The triple mutant YT478 ( Gln225→stop codon, K56R, and R485H), generated by screening for resistance to streptomycin and rifampin, expressed a 1,100-fold-larger amount of the extracellular enzyme cycloisomaltooligosaccharide glucanotransferase (CITase) than the wild-type strain. These mutants were characterized by higher intracellular -adenosylmethionine concentrations during exponential phase and enhanced protein synthesis activity during stationary phase. Surprisingly, the maximal expression of CITase mRNA was similar in the wild-type and triple mutant strains, but the mutant showed greater CITase mRNA expression throughout the growth curve, resulting in enzyme overproduction. A metabolome analysis showed that the triple mutant YT478 had higher levels of nucleic acids and glycolysis metabolites than the wild type, indicating that YT478 mutant cells were activated. The production of CITase by the triple mutant was further enhanced by introducing a mutation conferring resistance to the rare earth element, scandium. This combined drug resistance mutation method also effectively enhanced the production of amylases, proteases, and agarases by and This method also activated the silent or weak expression of the CITase gene, as shown by comparisons of the CITase gene loci of T-3040 and another cycloisomaltooligosaccharide-producing bacterium, sp. strain 598K. The simplicity and wide applicability of this method should facilitate not only industrial enzyme production but also the identification of dormant enzymes by activating the expression of silent or weakly expressed genes. Enzyme use has become more widespread in industry. This study evaluated the molecular basis and effectiveness of ribosome engineering in markedly enhancing enzyme production (>1,000-fold). This method, due to its simplicity, wide applicability, and scalability for large-scale production, should facilitate not only industrial enzyme production but also the identification of novel enzymes, because microorganisms contain many silent or weakly expressed genes which encode novel antibiotics or enzymes. Furthermore, this study provides a new mechanism for strain improvement, with a consistent rather than transient high expression of the key gene(s) involved in enzyme production.

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Enhanced lipase production by mutation induced Aspergillus japonicus

Cited by 28 publications

References 7 publications

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Strategies for the Development of Industrial Fungal Producing Strains

Combined Drug Resistance Mutations Substantially Enhance Enzyme Production in Paenibacillus agaridevorans

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