دورية أكاديمية
أعرض في EDS

Production Process Optimization of Recombinant Erwinia carotovora l-Asparaginase II in Escherichia coli Fed-Batch Cultures and Analysis of Antileukemic Potential.

التفاصيل البيبلوغرافية
العنوان: Production Process Optimization of Recombinant Erwinia carotovora l-Asparaginase II in Escherichia coli Fed-Batch Cultures and Analysis of Antileukemic Potential.
المؤلفون: de Andrade BC; National Institute of Science and Technology in Tuberculosis, Research Center for Molecular and Functional Biology, Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil.; Graduate Program in Medicine and Health Sciences, Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil., Renard G; Quatro G Pesquisa & Desenvolvimento Ltd., Porto Alegre, Rio Grande do Sul 90619-900, Brazil., Gennari A; Food Biotechnology Laboratory, Biotechnology Graduate Program, University of Vale do Taquari (UNIVATES), Lajeado, Rio Grande do Sul 95914-014, Brazil., Artico LL; Centro Infantil Boldrini, Campinas, São Paulo 13083-210, Brazil.; Graduate Program in Genetics and Molecular Biology, Biology Institute, State University of Campinas, Campinas, São Paulo 13083-970, Brazil., Júnior JRT; Centro Infantil Boldrini, Campinas, São Paulo 13083-210, Brazil.; Graduate Program in Genetics and Molecular Biology, Biology Institute, State University of Campinas, Campinas, São Paulo 13083-970, Brazil., Kuhn D; Food Biotechnology Laboratory, Biotechnology Graduate Program, University of Vale do Taquari (UNIVATES), Lajeado, Rio Grande do Sul 95914-014, Brazil., Salles PPZ; Centro Infantil Boldrini, Campinas, São Paulo 13083-210, Brazil.; Graduate Program in Genetics and Molecular Biology, Biology Institute, State University of Campinas, Campinas, São Paulo 13083-970, Brazil., Volken de Souza CF; Food Biotechnology Laboratory, Biotechnology Graduate Program, University of Vale do Taquari (UNIVATES), Lajeado, Rio Grande do Sul 95914-014, Brazil., Roth G; Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil., Chies JM; Quatro G Pesquisa & Desenvolvimento Ltd., Porto Alegre, Rio Grande do Sul 90619-900, Brazil., Yunes JA; Centro Infantil Boldrini, Campinas, São Paulo 13083-210, Brazil.; Department of Medical Genetics, Faculty of Medical Sciences, State University of Campinas, Campinas, São Paulo 13083-970, Brazil., Basso LA; National Institute of Science and Technology in Tuberculosis, Research Center for Molecular and Functional Biology, Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil.; Graduate Program in Medicine and Health Sciences, Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil.; Graduate Program in Cellular and Molecular Biology, Pontifical Catholic University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900, Brazil.
المصدر: ACS omega [ACS Omega] 2024 Aug 03; Vol. 9 (32), pp. 34951-34963. Date of Electronic Publication: 2024 Aug 03 (Print Publication: 2024).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101691658 Publication Model: eCollection Cited Medium: Internet ISSN: 2470-1343 (Electronic) Linking ISSN: 24701343 NLM ISO Abbreviation: ACS Omega Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, [2016]-
مستخلص: The aims of this work were to optimize the production of Erwinia carotovora l-asparaginase II enzyme in Escherichia coli by different fed-batch cultivation strategies using a benchtop bioreactor and to evaluate the therapeutic potential of the recombinant enzyme against different acute lymphoblastic leukemia cell lines. The highest enzyme activities (∼98,000 U/L) were obtained in cultures using the DO-stat feeding strategy with induction in 18 h of culture. Under these experimental conditions, the maximum values for recombinant l-asparaginase II (rASNase) yield per substrate, rASNase yield per biomass, and productivity were approximately 1204 U/g glucose , 3660 U/g cells , and 3260 U/(L·h), respectively. This condition was efficient for achieving high yields of the recombinant enzyme, which was purified and used in in vitro antileukemic potential tests. Of all the leukemic cell lines tested, RS4;11 showed the highest sensitivity to rASNase, with an IC 50 value of approximately 0.0006 U/mL and more than 70% apoptotic cells. The study demonstrated that the cultivation strategies used were efficient for obtaining high yield and productivity of rASNase with therapeutic potential inasmuch as cytotoxic activity and induction of apoptosis were demonstrated for this protein.
Competing Interests: The authors declare no competing financial interest.
(© 2024 The Authors. Published by American Chemical Society.)
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تواريخ الأحداث: Date Created: 20240819 Latest Revision: 20240820
رمز التحديث: 20240820
مُعرف محوري في PubMed: PMC11325515
DOI: 10.1021/acsomega.4c04711
PMID: 39157126
قاعدة البيانات: MEDLINE
الوصف
تدمد:2470-1343
DOI:10.1021/acsomega.4c04711