A comprehensive review on microbial <scp>l</scp>‐asparaginase: Bioprocessing, characterization, and industrial applications

Chand, Subhash; Mahajan, Richi V.; Prasad, Jai Prakash; Sahoo, Debendra K.; Mihooliya, Kanti N.; Dhar, Mahesh Shanker; Sharma, Girish

doi:10.1002/bab.1888

Cited by 81 publications

(53 citation statements)

References 129 publications

(219 reference statements)

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“…In addition to medical applications, large quantities of L-asparaginases are used in food manufacturing. The enzyme, purified from different strains of Aspergillus (e.g., A. oryzae), has been shown to be helpful in reducing buildup of acrylamide in foods such as coffee, biscuits, and potato chips [40][41][42]. Due to the absence of structural data for enzymes used by food industry, they will not be discussed further in this review.…”

Section: Utilization Of Asnases For Anticancer Therapy and Food Manufacturingmentioning

confidence: 99%

Structural and biochemical properties of L‐asparaginase

Łubkowski

Wlodawer

2021

The FEBS Journal

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L-asparaginase (a hydrolase converting L-asparagine to L-aspartic acid) was the first enzyme to be used in clinical practice as an anticancer agent after its approval in 1978 as a component of a treatment protocol for childhood acute lymphoblastic leukemia (ALL). Structural and biochemical properties of L-asparaginases have been extensively investigated during the last half century, providing an accurate structural description of the enzyme isolated from a variety of sources, as well as clarifying the mechanism of its activity. This review provides a critical assessment of the current state of knowledge of primarily structural, but also selected biochemical properties of "bacterial-type" L-asparaginases from different organisms. The most extensively studied members of this enzyme family are L-asparaginases highly homologous to one of the two enzymes from Escherichia coli (usually referred to as EcAI and EcAII). Members of this enzyme family, although often called bacterial-type L-asparaginases, have been also identified in such divergent organisms as archaea or eukarya. Over 100 structural models of L-asparaginases have been deposited in the Protein Data Bank during the last 30 years. One of the prime achievements of structure-centered approaches was the elucidation of the details of the mechanism of enzymatic action of this unique hydrolase that utilizes a side chain of threonine as the primary nucleophile. The molecular basis of other important properties of these enzymes, such as their substrate specificity, are still being evaluated. Results of structural and mechanistic studies of L-asparaginases are being utilized in efforts to improve the clinical properties of this important anticancer drug.

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Section: Utilization Of Asnases For Anticancer Therapy and Food Manufacturingmentioning

confidence: 99%

Structural and biochemical properties of L‐asparaginase

Łubkowski

Wlodawer

2021

The FEBS Journal

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“…Actinomycin D can be inserted into the DNA double helix to form a covalent bond, destroy the DNA template function, hinder DNA replication, transcription and translation and other functions, and interfere with rRNA transcription and protein synthesis [61]. L-asparaginase is an important enzyme that can hydrolyze L-asparagine, a key raw material for tumor protein synthesis, to L-aspartate, which leads to the inhibition of tumor protein synthesis [62]. Some chemotherapeutic drugs can destroy cell structural components such as cell membranes, organelles, and biological macromolecules.…”

Section: The Action Mechanism Of the Commonly Used Chemotherapeutic Drugsmentioning

confidence: 99%

Co-delivery of chemotherapeutic drugs and cell cycle regulatory agents using nanocarriers for cancer therapy

Sun

Jing

et al. 2021

Sci. China Mater.

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Combination chemotherapy is widely exploited to overcome multidrug resistance (MDR) and enhance the therapeutic effect of anti-tumor agents clinically. The traditional combination regimens applied in clinical practice still suffer from various obstacles, such as inevitable side effects. Fortunately, the application of nanotechnology and the proposal of co-delivery systems make the combination therapy more effective. The occurrence, development, and metastasis of tumors are closely related to the cell cycle. The sensitivity of tumor cells to chemotherapeutic drugs can be improved with the cooperation of cell cycle regulators. In this review, the influence of the cell cycle on tumorigenesis and development is introduced briefly. The current strategies of combining chemotherapeutic drugs and cell cycle regulators through codelivery systems are discussed in detail. We also sketch the possibility of treating tumors mildly via artificially controlling the cell cycle and outline the challenges and perspectives about the improvement of co-delivery systems for cancer therapy.

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“…Currently, there are few type II ASNase commercially available that have been produced industrially for medical applications (detailed in Table 1): (i) native ASNase from E. coli (Elspar ® from Ovation Pharmaceuticals, Illinois, IL, USA [52]; Leukanase ® from Sanofi-aventis, New South Wales, Australia; Kidrolase ® from EUSA Pharma, SAS, Lyon, France [53], etc. ); (ii) PEGylated ASNase from recombinant E. coli, pegaspargase (Oncaspar ® from Enzon Pharmaceuticals, Florida, FL, USA) [54]; (iii) native ASNase, but as a recombinant form, being produced in E. coli and E. chrysanthemi as host cells (Spectrila ® from Medac Gesellschaft, Wedel, Germany [55] and Erwinase ® (from Erwinia chrysanthemi) from EUSA Pharma, SAS, Lyon, France [56], respectively).…”

Section: Commercial Asnasementioning

confidence: 99%

Recent Strategies and Applications for l-Asparaginase Confinement

et al. 2020

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l-asparaginase (ASNase, EC 3.5.1.1) is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application.

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A comprehensive review on microbial l‐asparaginase: Bioprocessing, characterization, and industrial applications

Cited by 81 publications

References 129 publications

Structural and biochemical properties of L‐asparaginase

Structural and biochemical properties of L‐asparaginase

Co-delivery of chemotherapeutic drugs and cell cycle regulatory agents using nanocarriers for cancer therapy

Recent Strategies and Applications for l-Asparaginase Confinement

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