Recent Development in the Uses of Asparaginase as Food Enzyme

Alam, Shahenvaz; Pranaw, Kumar; Tiwari, Rameshwar; Khare, Sunil Kumar

doi:10.1007/978-981-13-3263-0_5

Cited by 20 publications

(9 citation statements)

References 108 publications

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“…The therapeutic enzymes of greatest global production include L-asparaginase (L-ASNase), which contributes 40% of the total global demand for enzymes and a third of the world's requirement as an antileukemic and antilymphoma agent, making it one of the enzymatic products with major industrial potential (Chand et al, 2020). ln 2017, global demand for this enzyme was USD 380m and it is estimated to reach USD 420m by 2025 (Alam et al, 2019). According to Chand et al (2020), L-ASNase is an amidohydrolase enzyme (EC3.5.1.1), widely recognized as one of the anticancer drugs with great potential due to its property of hydrolyzing L-asparagine into L-aspartate and ammonia, which inhibits protein synthesis in T-cells, making it a key chemotherapeutic agent for the treatment of acute lymphoblastic leukemia (ALL) and lymphosarcoma.…”

Section: Introductionmentioning

confidence: 99%

Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems

Lefin

Miranda

Beltrán

et al. 2022

Preprint

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L-asparaginase is one of the world’s most in-demand industrial enzymes, mainly due to its therapeutic properties and its use in the food industry. Over the years studies have been conducted to improve its specific activity and reduce side effects, driving new discoveries that promise safer, more efficient, and cheaper drugs for consumers. However, heterologous protein modifications or expression continue to be a problem during production. Therefore, addressing bottlenecks when attempting to express modified and/or heterologous proteins using the rational design of heterologous expression systems with modified hosts could be a promising strategy to improve L-asparaginase production. Problems such as inadequate protein folding, metabolic load on host cells, codon usage bias, repetitive sequences affecting translation, heavy molecular weight and/or multi-membrane domains formation; need great attention during the development of “bio-better” proteins. In this article, we address the current molecular and metabolic strategies that have been developed to improve the heterologous expression of L-asparaginase.

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Section: Introductionmentioning

confidence: 99%

Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems

Lefin

Miranda

Beltrán

et al. 2022

Preprint

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“…Acrylamide is formed by a mirrored reaction that occurs at extreme temperatures between asparagine and carbonyl compounds. The temperature for acrylamide production usually exceeds 100 ° C (Alam et al, 2019). Acrylamide is found in baked goods, fried foods and starchy foods because asparagine is the main cause of acrylamide formation.…”

Section: Introductionmentioning

confidence: 99%

“…The rasparaginase enzyme is considered to be the most important enzyme for its role in lymphoblast therapy and its inhibition of acrylamide production as a side reaction during industrial food processing (Narta et al, 2007). The importance of this enzyme is also demonstrated by its high global demand, which reached US $ 380 million in 2017 and is projected to increase to US $ 420 million by 2025 (10). Due to the important health and industrial importance of this enzyme, rasparaginase is currently being investigated for its powerful role in various types of cancer, including breast cancer (14).…”

Section: Introductionmentioning

confidence: 99%

L-Asparaginase, a promising enzyme in food industry

saadzaghloul

El-Sayed

yassen

et al. 2022

Bulletin of Faculty of Science, Zagazig University

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L-Asparaginase is an effective chemotherapeutic enzyme catalyzes hydrolysis of the amino acid asparagine into aspartate and ammonia which is essential for tumour cells. It has been effectively used in the treatment of acute lymphoblastic leukemia and lymphosarcoma. Acrylamide, the low molecular weight human carcinogen, has neurotoxic and genotoxic effects. The mechanism behind the inhibition of acrylamide generation in food systems are the hydrolysis of carboxamide group of amine in asparagine into asparatic acid and this lead to either elimination or reduction in acrylamide content in food. Utilizing of Lasparaginase as a mitigation technique for reduced acrylamide concentration is the main promising application in food industry. The present review focuses on enzyme sources, mechanism of action as well as a detailed information about its production and purification. It also provides some recent updated information about its chemical structure, physiochemical, kinetic properties of the enzyme and its applications in food industry.

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“…Acrylamide (ACR) was first identified in food products by a Swedish scientist [1], as starch-based foods were often cooked above 120 • C [2]. ACR has been marked as a Group 2A carcinogen, according to the International Agency for Research on Cancer [3]. Since its discovery in foodstuffs, the subject of the toxicity and metabolism of ACR has become a topic of debate.…”

Section: Introductionmentioning

confidence: 99%

A Chemosensor Based on Gold Nanoparticles and Dithiothreitol (DTT) for Acrylamide Electroanalysis

et al. 2021

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Rapid and simple electroanalysis of acrylamide (ACR) was feasible by a gold electrode modified with gold nanoparticles (AuNPs) and dithiothreitol (DTT) with enhanced detection sensitivity and selectivity. The roughness of bare gold (Au) increased from 0.03 μm to 0.04 μm when it was decorated with AuNPs. The self-assembly between DTT and AuNPs resulted in a surface roughness of 0.09 μm. The DTT oxidation occurred at +0.92 V. The Au/AuNPs/DTT surface exhibited a surface roughness of 0.24 μm after its exposure to ACR with repeated analysis. SEM imaging illustrated the formation of a polymer layer on the Au/AuNPs/DTT surface. Surface plasmon resonance analysis confirmed the presence of AuNPs and DTT on the gold electrode and the binding of ACR to the electrode’s active surface area. The peak area obtained by differential pulse voltammetry was inversely proportional to the ACR concentrations. The limit of detection (LOD) and the limit of quantitation (LOQ) were estimated to be 3.11 × 10−9 M and 1 × 10−8 M, respectively, with wide linearity ranging from 1 × 10−8 M to 1 × 10−3 M. The estimated levels of ACR in potato chips and coffee samples by the sensor were in agreement with those of high-performance liquid chromatography.

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Recent Development in the Uses of Asparaginase as Food Enzyme

Cited by 20 publications

References 108 publications

Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems

Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems

L-Asparaginase, a promising enzyme in food industry

A Chemosensor Based on Gold Nanoparticles and Dithiothreitol (DTT) for Acrylamide Electroanalysis

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