Optimization of culture conditions and bench-scale production of anticancer enzyme L-asparaginase by submerged fermentation from<i>Aspergillus terreus</i>CCT 7693

Costa-Silva, Tales A.; Camacho-Córdova, D I; Montalvo, Gualberto Segundo Agamez; Parizotto, L; Sánchez‐Moguel, Ignacio; Pessoa, Adalberto

doi:10.1080/10826068.2018.1536990

Cited by 16 publications

(8 citation statements)

References 25 publications

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“…Temperature not only affects the physical properties of the fermentation broth but also affects the properties of protein and the reaction rate of enzymes ( Prentice et al, 2020 ). In addition, the enzyme activity of the fermentation broth gradually decreases, which may be since the temperature is too high, which leads to the easy aging of the strain and affects its growth and metabolism, thereby inhibiting its fermentation and enzyme production ( Wang et al, 2016 ; Costa-Silva et al, 2019 ).…”

Section: Discussionmentioning

confidence: 99%

In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein

Wang,

Jiang,

Liu

et al. 2023

Front. Bioeng. Biotechnol.

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Introduction: Trehalose is a significant rare sugar known for its stable properties and ability to protect biomolecules from environmental factors.Methods: In this study, we present a novel approach utilizing a scaffold protein-mediated assembly method for the formation of a trehalose bi-enzyme complex. This complex consists of maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase), which work in tandem to catalyze the substrate and enhance the overall catalytic efficiency. Utilizing the specific interaction between cohesin and dockerin, this study presents the implementation of an assembly, an analysis of its efficiency, and an exploration of strategies to enhance enzyme utilization through the construction of a bi-enzyme complex under optimal conditions in vitro.Results and Discussion: The bi-enzyme complex demonstrated a trehalose production level 1.5 times higher than that of the free enzyme mixture at 40 h, with a sustained upward trend. Compared to free enzyme mixtures, the adoption of a scaffold protein-mediated bi-enzyme complex may improve cascade reactions and catalytic effects, thus presenting promising prospects.

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Section: Discussionmentioning

confidence: 99%

In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein

Wang,

Jiang,

Liu

et al. 2023

Front. Bioeng. Biotechnol.

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“…Compared to plant and animal sources, microbes are more cost-effective and easier to modify, optimize, extract, and purify for enzyme synthesis ( Fazeli et al, 2021 ). In addition, genetically altering microbes to boost yields is simple ( Costa-Silva et al, 2019 ). Because bacterial and fungal L-asparaginases are thought to be important in both medicine and industry, this review focuses on their kinetic properties.…”

Section: Kinetic Parameters Of Microbial L-asparaginases In Recent St...mentioning

confidence: 99%

“…To reduce these immunological issues, a different supply is required. Fungi have evolved more closely with humans than bacteria, so it is likely that the enzymes they produce will have lower immunogenicity than bacteria ( Ashok et al, 2019 ; Costa-Silva et al, 2019 ).…”

Section: Kinetic Parameters Of Fungi-derived L-asparaginasesmentioning

confidence: 99%

Desirable L-asparaginases for treating cancer and current research trends

Tsegaye,

Tsehai,

Getie

2024

Front. Microbiol.

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Amino acid depletion therapy is a promising approach for cancer treatment. It exploits the differences in the metabolic processes between healthy and cancerous cells. Certain microbial enzymes induce cancer cell apoptosis by removing essential amino acids. L-asparaginase is an enzyme approved by the FDA for the treatment of acute lymphoblastic leukemia. The enzymes currently employed in clinics come from two different sources: Escherichia coli and Erwinia chrysanthemi. Nevertheless, the search for improved enzymes and other sources continues because of several factors, including immunogenicity, in vivo instability, and protease degradation. Before determining whether L-asparaginase is clinically useful, research should consider the Michaelis constant, turnover number, and maximal velocity. The identification of L-asparaginase from microbial sources has been the subject of various studies. The primary goals of this review are to explore the most current approaches used in the search for therapeutically useful L-asparaginases and to establish whether these investigations identified the crucial characteristics of L-asparaginases before declaring their therapeutic potential.

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“…Currently, three different approaches are used for enzyme bioengineering: semi-rational, directed evolution, and rational design, depending on the level of information available about the sequence, structure and function of the target enzyme [23]. To improve the various properties of L-ASNases, researchers have used rational design and other molecular approaches [16,[24][25][26][27][28][29][30][31][32][33][34][35][36][37]. Rational design methods have been useful in predicting and modifying enzyme structures.…”

Section: Of 60mentioning

confidence: 99%

Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production

Shishparenok,

Gladilina,

Zhdanov

2023

IJMS

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Genetic engineering for heterologous expression has advanced in recent years. Model systems such as Escherichia coli, Bacillus subtilis and Pichia pastoris are often used as host microorganisms for the enzymatic production of L-asparaginase, an enzyme widely used in the clinic for the treatment of leukemia and in bakeries for the reduction of acrylamide. Newly developed recombinant L-asparaginase (L-ASNase) may have a low affinity for asparagine, reduced catalytic activity, low stability, and increased glutaminase activity or immunogenicity. Some successful commercial preparations of L-ASNase are now available. Therefore, obtaining novel L-ASNases with improved properties suitable for food or clinical applications remains a challenge. The combination of rational design and/or directed evolution and heterologous expression has been used to create enzymes with desired characteristics. Computer design, combined with other methods, could make it possible to generate mutant libraries of novel L-ASNases without costly and time-consuming efforts. In this review, we summarize the strategies and approaches for obtaining and developing L-ASNase with improved properties.

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Optimization of culture conditions and bench-scale production of anticancer enzyme L-asparaginase by submerged fermentation fromAspergillus terreusCCT 7693

Cited by 16 publications

References 25 publications

In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein

In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein

Desirable L-asparaginases for treating cancer and current research trends

Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production

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