Biochemical Characterization of a Novel
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            -Asparaginase with Low Glutaminase Activity from Rhizomucor miehei and Its Application in Food Safety and Leukemia Treatment

Huang, Linhua; Liu, Yu; Sun, Yan; Yan, Qiaojuan; Jiang, Zhengqiang

doi:10.1128/aem.03523-13

Cited by 93 publications

(37 citation statements)

References 34 publications

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“…This is because the enzyme reduces more than 88% of the l -asparagine concentration from the initial feedstock. In last years, other works have dealt with this application of l -asparaginase, that can decrease the negative effects of acrylamide containing foods without impair their characteristics 3, 25, 26, 27, 28…”

Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

171

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l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

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Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

171

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“…33,34 Because asparagine is also a key precursor in the formation of acrylamide, several studies have examined the potential of asparaginases from microbial sources to reduce the acrylamide content of processed foods, reviewed by Anese et al 35 and Zuo et al 36 These include the following selected observations. Blast cells lack the ability to synthesize the amino acid L-asparagine and rely on other sources of L-asparagine for protein synthesis.…”

Section: Asparaginases Inhibit Acrylamide Formation In Foodmentioning

confidence: 99%

Acrylamide: inhibition of formation in processed food and mitigation of toxicity in cells, animals, and humans

Friedman

2015

Food Funct.

117

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Potentially toxic acrylamide is largely derived from the heat-inducing reactions between the amino group of the amino acid asparagine and carbonyl groups of glucose and fructose in plant-derived foods including cereals, coffees, almonds, olives, potatoes, and sweet potatoes. This review surveys and consolidates the following dietary aspects of acrylamide: distribution in food, exposure and consumption by diverse populations, reduction of the content in different food categories, and mitigation of adverse in vivo effects. Methods to reduce acrylamide levels include selecting commercial food with a low acrylamide content, selecting cereal and potato varieties with low levels of asparagine and reducing sugars, selecting processing conditions that minimize acrylamide formation, adding food-compatible compounds and plant extracts to food formulations before processing that inhibit acrylamide formation during processing of cereal products, coffees, teas, olives, almonds, and potato products, and reducing multiorgan toxicity (antifertility, carcinogenicity, neurotoxicity, teratogenicity). The herein described observations and recommendations are of scientific interest for food chemistry, pharmacology, and toxicology, but also have the potential to benefit nutrition, food safety, and human health.

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“…Studies have demonstrated the production of l ‐ASNase with low l ‐GLUase activity from eukaryotic sources (Huang et al . ; Doriya and Kumar ), although some studies have shown that l ‐GLUase activity is important for the overall efficacy of treatment and serves as a positive modulator of l ‐ASNase activity in sub‐micromolar concentrations of asparagine in the serum of patients undergoing treatment (Anishkin et al . ).…”

Section: Discussionmentioning

confidence: 99%

Screening and optimizing fermentation production ofl‐asparaginase byAspergillus terreusstrain S‐18 isolated from the Brazilian Caatinga Biome

Rocha

Costa-Silva

Montalvo³

et al. 2019

J Appl Microbiol

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Aims The aim of this study was to find new eukaryotic sources of the l‐asparaginase (l‐ASNase), since the prokaryotic sources of the enzyme are well‐reported as causing allergic hypersensitivity reactions in a significant number of patients. This report describes screening for l‐ASNase production by filamentous fungi isolated from the Brazilian Caatinga, and the optimization of fermentation parameters to increase fungal growth and improve yield in the production of l‐ASNase. Methods and Results Thirty‐two filamentous fungi were investigated in this study. When Aspergillus terreus strain S‐18 was cultured in a proline‐enriched medium, intracellular l‐ASNase was expressed in concurrence with reduced l‐glutaminase (l‐GLUase) and protease activities. Fermentation conditions were then optimized in a 5‐l bioreactor system to produce a maximum volumetric yield of 108 U total of l‐ASNase activity. Conclusions The work reported here represents the first attempt to produce l‐ASNase by filamentous fungi isolated from Brazil and offers a promising alternative eukaryotic source for l‐ASNase production. Significance and Impact of the study In order to minimize the side effects caused by bacterial l‐ASNase, the search of eukaryotic micro‐organism for l‐ASNase was carried out in fungi. This study demonstrates the diversity of filamentous fungi isolated from the Brazilian Caatinga Biome and the importance of knowledge of the microbial metabolism to obtain high concentrations of biotechnological products.

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Biochemical Characterization of a Novel l -Asparaginase with Low Glutaminase Activity from Rhizomucor miehei and Its Application in Food Safety and Leukemia Treatment

Cited by 93 publications

References 34 publications

Current applications and different approaches for microbial l-asparaginase production

Current applications and different approaches for microbial l-asparaginase production

Acrylamide: inhibition of formation in processed food and mitigation of toxicity in cells, animals, and humans

Screening and optimizing fermentation production ofl‐asparaginase byAspergillus terreusstrain S‐18 isolated from the Brazilian Caatinga Biome

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