Acute lymphoblastic leukemia (ALL) is a neoplastic disease characterized by the malignant proliferation of lymphoid cells in the blood and bone marrow. It accounts for approximately 75% of childhood leukemia. Lymphoblastic lymphoma (LBL) is a type of non-Hodgkin's lymphoma characterized by rapid growth and highly aggressive characteristics that occurs most commonly in adolescents and young adults. Asparaginase is primarily used to treat patients with ALL or LBL. Because allergic reactions occur in patients treated with bacterial-derived asparaginase, it is important to develop an alternative asparaginase preparation for patients allergic to asparaginase. Recombinant asparaginase -rywn (JZP-458) is a recombinant asparaginase that uses a novel expression platform in the production process. JZP-458 has the same amino acid sequence as -derived asparaginase (ERW) and its in vitro activity is similar to that of ERW. JZP-458 is highly efficacious in patients allergic to asparaginase. Data from a phase I clinical trial indicated that following the intramuscular or intravenous administration of JZP-458 to volunteers, serum asparaginase activity ≥ 0.1 IU/mL was observed in 100% of the volunteers 72 hours after administration. In this review, we summarize the mechanism of action and the related research data obtained with JZP-458 for the treatment of ALL or LBL.
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http://dx.doi.org/10.1358/dot.2022.58.6.3413459 | DOI Listing |
Prep Biochem Biotechnol
January 2025
Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran.
L-asparaginase (asparagine amidohydrolase) contributes to 40% of the total enzyme demands worldwide and is one-third of the global requirement as an anti-cancerous drug in treating acute lymphocytic leukemia (ALL), a type of leukemia. This protein breaks down L-asparagine into aspartic acid and ammonia those involved in ALL, rely on for growth and survival. Both non-recombinant and recombinant L-asparaginase can be produced by bacteria when a suitable substrate and method (solid-state fermentation (SSF) or submerged fermentation (SmF) which are techniques to grow microorganisms under controlled conditions), is provided.
View Article and Find Full Text PDFFood Chem
January 2025
Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai-400 019, India. Electronic address:
L-Asparaginase CLEAs were prepared utilizing sodium tripolyphosphate (TPP) as a crosslinker (TA-CLEA). Under optimized conditions (pH 3, 0.3% TPP concentration, and a crosslinking time of 1 h), an 85% activity recovery was achieved.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
State Key Laboratory of Geohazard Prevention and Geoenvironment Protection, Chengdu University of Technology, Chengdu 610059, China. Electronic address:
The increasing environmental concerns and health risks associated with synthetic chemicals have driven the demand for sustainable and eco-friendly solutions. Biocatalysis, employing enzymes or whole cells as biocatalysts, has emerged as a powerful alternative. This review provides a comprehensive analysis of the applications of biocatalytic enzymes in food packaging, biomedical sciences, and biotechnology.
View Article and Find Full Text PDFCurr Microbiol
January 2025
Applied Phycology and Biotechnology Division, CSIR-Central Salt and Marine Chemicals Research Institute, Bhavnagar, 364001, India.
The present study explores the microbial community associated with the industrially important red seaweed Gracilaria dura to determine the diversity and biotechnological potential through culture and metagenomics approaches. In the first part of the investigation, we isolated and characterized 75 bacterial morphotypes, with varied colony characteristics and metabolic diversity from the wild seaweed. Phylogenetic analysis identified isolates in Proteobacteria, Firmicutes, and Actinobacteria, with Bacillus sp.
View Article and Find Full Text PDFBioconjug Chem
January 2025
Department of Biochemistry, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.
l-Asparaginase (l-ASNase) catalyzes the hydrolysis of l-asparagine, leading to its depletion and subsequent effects on the cellular proliferation and survival. In contrast to normal cells, malignant cells that lack asparagine synthase are extremely susceptible to asparagine deficiency. l-ASNase has been successfully employed in treating pediatric leukemias and non-Hodgkin lymphomas; however, its usage in adult patients and other types of cancer is limited due to significant side effects and drug resistance.
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