l-asparaginase: Need for an Expedition from an Enzymatic Molecule to Antimicrobial Drug

Vimal, Archana; Kumar, Awanish

doi:10.1007/s10989-021-10312-x

Cited by 11 publications

(4 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Among 4409 protein-coding sequences identified in this strain, some genes encode enzymes for polysaccharide and protein degradation known to exhibit anti-biofilm properties against pathogenic bacteria [57]. Notable examples are protease [50], chitinase [12], a mixture of bacillolysin and subtilisin (Protamex ® ) [20,48], L-asparaginase [64,65], and pullulanase [51] (Table 1). From the ecological point of view, the presence of these genes suggests that HI03-3b may produce antimicrobial or anti-biofilm enzymes in competing for nutrient and space against other epibionts as well as in protecting algal host from predation [17,18].…”

Section: Discussionmentioning

confidence: 99%

Biotechnologically potential genes in a polysaccharide-degrading epibiont of the Indonesian brown algae Hydroclathrus sp.

Ethica

Zilda²,

Oedjijono

et al. 2023

Journal of Genetic Engineering and Biotechnology

View full text Add to dashboard Cite

Background Marine bacteria have recently attracted increasing attention to be harnessed for the production of valuable enzymes, vitamins, and bioactive compounds. Bacteria associated with the surfaces of marine macroalgae, called epibionts, are particularly interesting from ecological and biotechnological points of view, as they often exhibit antimicrobial activities to compete with pathogenic bacteria for nutrients and spaces. In search for biotechnologically potential genes from marine bacteria, we sequenced and analysed the genome of the epibiont HI03-3b, a polysaccharide-degrading bacterium associated with the surface of the Indonesian brown algae Hydroclathrus sp. Results The algal epibiont HI03-3b has a genome of approximately 4,860,704 bp in size with 42.02 mol% G + C content, consisting of 5655 open reading frames (ORFs), 4409 genes coding for proteins (CDSs), 94 genes for tRNAs, and 32 genes for rRNAs. The genome sequence of HI03-3b was most closely related to that of Cytobacillus firmus NCTC10335 with the average amino acid identity (AAI) of 95.0 %, average nucleotide identity (ANI) of 94.1 %, and a recommended DNA-DNA hybridization (DDH) of 57.60 %. These scores are lower than the most frequently used standard for species demarcation (95% ANI cutoff) and the new species threshold (DDH > 70.0% for the same bacterial species). Some differences in genome features and gene composition were observed between HI03-3b and NCTC10335, such as genes encoding carbohydrate active enzymes. These suggest that HI03-3b is unique and likely a novel species within Cytobacillus genus, and we therefore proposed its name as Cytobacillus wakatobiense HI03-3b. Genome sequence analyses indicated the presence of genes involved not only in polysaccharide and protein degradation but also in vitamin and secondary metabolite biosynthesis. Some of them encode enzymes and compounds with biotechnological interest, such as protease, chitinase, subtilisin, pullulanase, and bacillolysin, which are often associated with antimicrobial or antibiofilm activities. This antimicrobial potential is supported by our finding that the extracellular protein fraction of this epibiont inhibited the growth of the bacterial pathogen Staphylococcus aureus. Conclusion The epibiont Cytobacillus HI03-3b harbours genes for polysaccharide and protein degradation as well as for natural product biosynthesis, suggesting its potential ecological roles in outcompeting other bacteria during biofilm formation as well as in protecting its algal host from predation. Due to the presence of genes for vitamin biosynthesis, it might also provide the algal host with vitamins for growth and development. Some of these metabolic genes are biotechnologically important, as they could become a platform for bioengineering to generate various seaweed-derived substances sustainably, such as antibiofilm agents and vitamins, which are beneficial for human health.

show abstract

Section: Discussionmentioning

confidence: 99%

Biotechnologically potential genes in a polysaccharide-degrading epibiont of the Indonesian brown algae Hydroclathrus sp.

Ethica

Zilda²,

Oedjijono

et al. 2023

Journal of Genetic Engineering and Biotechnology

View full text Add to dashboard Cite

show abstract

“…In recent years, there has been increasing interest in investigating the potential of this enzyme as an antibacterial agent. The antimicrobial activity of L-ASNase has been described against a wide range of gram-positive/gram-negative bacteria: Klebsiella pneumoniae, Listeria monocytogenes, Proteus vulgaris, Pseudomonas aeruginosa, Staphylococcus aureus, Salmonella typhimurium [22].…”

Section: Of 60mentioning

confidence: 99%

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

Shishparenok,

Gladilina,

Zhdanov

2023

IJMS

View full text Add to dashboard Cite

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.

show abstract

“…Kromě dlouhodobě využívané protinádorové aktivity byly nedávno u l-ASNas popsány možnosti využití i v dalších medicínských aplikacích 10 . Publikovány byly například studie upozorňující na potenciál l-ASNasy v léčbě infekčních a autoimunitních onemocnění 48 .…”

Section: Další Aplikace V Medicíněunclassified

ʟ-Asparaginases and Their Potential in Biotechnology and Medicine

Pejšková,

Loužecká,

Podzimek

et al. 2023

Chem. Listy

View full text Add to dashboard Cite

ʟ-Asparaginase (EC 3.5.1.1) is a key enzyme that hydrolyzes ʟ-asparagine to ʟ-aspartic acid and ammonia. This feature of ʟ-asparaginase is used in anti‑cancer therapy to inhibit protein synthesis in cancer cells. Therefore, ʟ-asparaginase is used as a basis for chemotherapy to treat patients with acute lymphoblastic leukemia in pediatrics. Commercial ʟ-asparaginases for healthcare applications are mainly obtained from Escherichia coli and Erwinia chrysanthemi (renamed to Dickeya dadantii). However, the high prevalence of adverse effects complicates the long‑term clinical use of ʟ-asparaginase, and therefore current research focuses on the search for new enzymes or on modifying the properties of enzymes already known. At the same time, ʟ-asparaginase has become indispensable for the food industry in recent years, when it had been recognized as one of the possible tools for removing ʟ-asparagine from foods that are at risk of acrylamide formation during thermal processing. This review provides an overview of the current use of ʟ-asparaginase and its pitfalls.

show abstract

l-asparaginase: Need for an Expedition from an Enzymatic Molecule to Antimicrobial Drug

Cited by 11 publications

References 18 publications

Biotechnologically potential genes in a polysaccharide-degrading epibiont of the Indonesian brown algae Hydroclathrus sp.

Biotechnologically potential genes in a polysaccharide-degrading epibiont of the Indonesian brown algae Hydroclathrus sp.

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

ʟ-Asparaginases and Their Potential in Biotechnology and Medicine

Contact Info

Product

Resources

About