Characterization of L-asparaginase from marine-derived Aspergillus niger AKV-MKBU, its antiproliferative activity and bench scale production using industrial waste

Vala, Anjana K.; Sachaniya, Bhumi K.; Dudhagara, Dushyant R.; Panseriya, Haresh Z.; Gosai, Haren B.; Rawal, Rakesh; Dave, Bharti P.

doi:10.1016/j.ijbiomac.2017.11.114

Cited by 66 publications

(33 citation statements)

References 32 publications

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“…Differently, the L-asparaginase activity was reduced in the presence of EDTA for the enzymes produced by A. niger AKV-MKBU and by R. miehei. 27,29 The A. niveus L-asparaginase was drastically reduced in the presence of SDS, as also observed by Vala et al, for the enzyme produced by A. niger AKV-MKBU. 29 The Talaromyces pinophilus enzyme was also inhibited in the presence of SDS.…”

Section: Effect Of Different Compounds On L-asparaginase Activitysupporting

confidence: 72%

“…27,29 The A. niveus L-asparaginase was drastically reduced in the presence of SDS, as also observed by Vala et al, for the enzyme produced by A. niger AKV-MKBU. 29 The Talaromyces pinophilus enzyme was also inhibited in the presence of SDS. 26 The SDS is a denaturing agent that can interact with hydrophobic regions of the enzyme promoting denaturation or aggregation.…”

Section: Effect Of Different Compounds On L-asparaginase Activitysupporting

confidence: 72%

“…Reduction of the L-asparaginase activity was also observed for the enzymes from A. niger AKV-MKBU, R. miehei and Cladosporium sp. 27,29,31 In the presence of organic solvents, the enzyme activity was inhibited only in the presence of acetone. Interestingly, the activation in the presence of other solvents is not dependent on the hydrophobicity of the compound.…”

Section: Effect Of Different Compounds On L-asparaginase Activitymentioning

confidence: 99%

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Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

Amatto

Guimarães

2019

Int J Sci Rep

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Background: L-asparaginase, produced mainly by microrganisms, cleaves L-asparagine to aspartic acid and ammonia as products. This enzyme has been applied in the treatment of the leukemia and in food preparation preventing the acrylamide formation.Methods: Aspergillus niveus was grown in different solid substrates (agroindustrial byproducts) moistened with different agents (tap water, distilled water and several salt solutions) for different periods (24-240 h) at 30ºC. The enzyme extract was obtained with the addition of cold distilled water, agitation at 50 rpm for 30 min and filtration. The filtrate was used to determine the L-asparaginase activity through the hydroximate aspartic methodology using L-asparagine as substrate. The influence of temperature (30-75ºC), pH (3-9) and chemical compounds on the enzyme activity was analyzed. Results: The highest level of enzyme production was obtained using the M1 mixture (wheat bran, crushed soybean, orange peel; 1:1:1, w/w/w) as substrate humidified with Czapeck Dox salt solution (1:0.5, m/v) for 48-120 h, at 30ºC. The best temperature and pH for the enzyme activity were 35ºC and 5.0, respectively. The enzyme activity was increased in the presence of NaCl and some organic solvents (acetonitrile, butanol ethanol, isopropanol and methanol).Conclusions: A. niveus produced L-asparaginase under SSF using a mixture of agroindustrial byproducts as solid substrate in the absence of L-asparagine as inducer. The temperature and pH of activity, as well as the NaCl tolerance, indicate its potential to be applied for different purposes. A. niveus can be an interesting source of L-asparaginase gene to be investigated targeting future application.

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Section: Effect Of Different Compounds On L-asparaginase Activitysupporting

confidence: 72%

Section: Effect Of Different Compounds On L-asparaginase Activitysupporting

confidence: 72%

Section: Effect Of Different Compounds On L-asparaginase Activitymentioning

confidence: 99%

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Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

Amatto

Guimarães

2019

Int J Sci Rep

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“…Several ASNase producing microorganisms have already been described in the literature, such as Escherichia coli, Dickeya chrysanthemi (previously known as Erwinia chrysanthemi), Saccharomyces cerevisiae, Aspergillus sp., Serratia marcescens, Proteus vulgaris among others, and screening work continues to find new ones (Rowley and Wriston, 1967; Tosa et al, 1971; Costa et al, 2016; Doriya and Kumar, 2016; Vimal and Kumar, 2017; Qeshmi et al, 2018; Vala et al, 2018). However, as previously mentioned, only the enzymes from E. coli and D. chrysanthemi are produced on an industrial scale for pharmaceutical use (Merck, 2000; European Medicines Agency, 2015, 2016; Medicines Evaluation Board, 2015).…”

Section: L-asparaginase Manufacturing: Production Process and Purificmentioning

confidence: 99%

Development of L-Asparaginase Biobetters: Current Research Status and Review of the Desirable Quality Profiles

Brumano

Silva

Costa-Silva

et al. 2019

Front. Bioeng. Biotechnol.

130

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L-Asparaginase (ASNase) is a vital component of the first line treatment of acute lymphoblastic leukemia (ALL), an aggressive type of blood cancer expected to afflict over 53,000 people worldwide by 2020. More recently, ASNase has also been shown to have potential for preventing metastasis from solid tumors. The ASNase treatment is, however, characterized by a plethora of potential side effects, ranging from immune reactions to severe toxicity. Consequently, in accordance with Quality-by-Design (QbD) principles, ingenious new products tailored to minimize adverse reactions while increasing patient survival have been devised. In the following pages, the reader is invited for a brief discussion on the most recent developments in this field. Firstly, the review presents an outline of the recent improvements on the manufacturing and formulation processes, which can severely influence important aspects of the product quality profile, such as contamination, aggregation and enzymatic activity. Following, the most recent advances in protein engineering applied to the development of biobetter ASNases (i.e., with reduced glutaminase activity, proteolysis resistant and less immunogenic) using techniques such as site-directed mutagenesis, molecular dynamics, PEGylation, PASylation and bioconjugation are discussed. Afterwards, the attention is shifted toward nanomedicine including technologies such as encapsulation and immobilization, which aim at improving ASNase pharmacokinetics. Besides discussing the results of the most innovative and representative academic research, the review provides an overview of the products already available on the market or in the latest stages of development. With this, the review is intended to provide a solid background for the current product development and underpin the discussions on the target quality profile of future ASNase-based pharmaceuticals.

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“…Thakur et al (2014) and Huang et al (2014) also reported that Mn 2+ is an activator for l-asparaginase from Mucor hiemalis and Rhizomucor miehei, respectively. On the other hand, Vala et al (2018) described that l-asparaginase of A. niger AKV-MKBU was inhibited by Mn 2+ at the concentration of 10 mM.…”

Section: Effect Of Metal Ions and Other Compounds On L-asparaginase Amentioning

confidence: 99%

l-Asparaginase from Aspergillus spp.: production based on kinetics, thermal stability and biochemical characterization

2019

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This study describes the production of native l-asparaginases by submerged fermentation from Aspergillus strains and provides the biochemical characterization, kinetic and thermodynamic parameters of the three ones that stood out for high l-asparaginase production. For comparison, the commercial fungal l-asparaginase was also studied. Both commercial and l-asparaginase from Aspergillus oryzae CCT 3940 showed optimum activity and stability in the pH range from 5 to 8 and the asparaginase from Aspergillus niger LBA 02 was stable in a more alkaline pH range. About the kinetic parameters, the denaturation constant increased with the heating temperature for all l-asparaginases, indicating that the l-asparaginase activity decreased at higher temperatures, especially above 60 °C. Moreover, l-asparaginase from A. oryzae CCT 3940 remained stable after 60 min at 50 °C. None of the l-asparaginases were inhibited by high NaCl concentrations, which are highly desirable for food industry application. The catalytic activities of all the l-asparaginases were enhanced by the presence of Mn 2+ and inhibited by p-chloromercuribenzoate and iodoacetamide. The l-asparaginase from the Aspergillus strains and the commercial enzyme had similar K m when l-asparagine was used as substrate. None of the l-asparaginases, except the l-asparaginase from A. niger LBA 02, could hydrolyze the substrate l-glutamine, which is of interest for medical proposes, since the glutaminase activity is usually related to adverse reaction during the leukemia treatment. This study showed that these new three non-recombinant l-asparaginases studied have potential application in the food and pharmaceutical industries, especially due to their good thermostability.

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Characterization of L-asparaginase from marine-derived Aspergillus niger AKV-MKBU, its antiproliferative activity and bench scale production using industrial waste

Cited by 66 publications

References 32 publications

Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

Development of L-Asparaginase Biobetters: Current Research Status and Review of the Desirable Quality Profiles

l-Asparaginase from Aspergillus spp.: production based on kinetics, thermal stability and biochemical characterization

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