دورية أكاديمية
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A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives.

التفاصيل البيبلوغرافية
العنوان: A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives.
المؤلفون: Siódmiak J; Department of Laboratory Medicine, Faculty of Pharmacy, Ludwik Rydygier Collegium Medicum, Nicolaus Copernicus University in Toruń, 85-094 Bydgoszcz, Poland., Dulęba J; Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.; Department of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, Poland., Kocot N; Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.; Doctoral School of Medical and Health Sciences, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland.; Department of Pharmaceutical Biochemistry, Faculty of Pharmacy, Jagiellonian University Medical College, Medyczna 9, 30-688 Kraków, Poland., Mastalerz R; Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland., Haraldsson GG; Science Institute, University of Iceland, 107 Reykjavik, Iceland., Marszałł MP; Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland., Siódmiak T; Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.; Department of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, Poland.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2024 May 07; Vol. 25 (10). Date of Electronic Publication: 2024 May 07.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Lipase*/chemistry , Lipase*/metabolism , Enzymes, Immobilized*/chemistry , Enzymes, Immobilized*/metabolism , Biocatalysis* , Fungal Proteins*/metabolism , Fungal Proteins*/chemistry , Sepharose*/chemistry, Propionates/chemistry ; Stereoisomerism ; Kinetics ; Esterification ; Temperature ; Enzyme Stability ; Candida/enzymology ; Solvents/chemistry ; Saccharomycetales
مستخلص: The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers of chiral drugs in reactions carried out in organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it is extremely important to develop optimal procedures to achieve a high enantioselectivity of the biocatalysts in the organic medium. Our paper describes a new approach to biocatalysis performed in an organic solvent with the use of CALB-octyl-agarose support including the application of a polypropylene reactor, an appropriate buffer for immobilization (Tris base-pH 9, 100 mM), a drying step, and then the storage of immobilized lipases in a climatic chamber or a refrigerator. An immobilized lipase B from Candida antarctica (CALB) was used in the kinetic resolution of ( R , S )-flurbiprofen by enantioselective esterification with methanol, reaching a high enantiomeric excess (ee p = 89.6 ± 2.0%). As part of the immobilization optimization, the influence of different buffers was investigated. The effect of the reactor material and the reaction medium on the lipase activity was also studied. Moreover, the stability of the immobilized lipases: lipase from Candida rugosa (CRL) and CALB during storage in various temperature and humidity conditions (climatic chamber and refrigerator) was tested. The application of the immobilized CALB in a polypropylene reactor allowed for receiving over 9-fold higher conversion values compared to the results achieved when conducting the reaction in a glass reactor, as well as approximately 30-fold higher conversion values in comparison with free lipase. The good stability of the CALB-octyl-agarose support was demonstrated. After 7 days of storage in a climatic chamber or refrigerator (with protection from humidity) approximately 60% higher conversion values were obtained compared to the results observed for the immobilized form that had not been stored. The new approach involving the application of the CALB-octyl-agarose support for reactions performed in organic solvents indicates a significant role of the polymer reactor material being used in achieving high catalytic activity.
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معلومات مُعتمدة: Excellence Initiative - Debuts, under the "Excellence Initiative-Research University" program, NCU in Toruń - 9/2022/Debiuty3 and 6/2022/Debiuty3 Nicolaus Copernicus University
فهرسة مساهمة: Keywords: (R,S)-flurbiprofen; climatic chamber; enantioselective esterification; immobilization; kinetic resolution; lipase B from Candida antarctica; lipase from Candida rugosa; octyl-Sepharose CL-4B; octyl-agarose; polypropylene; reactor material; storage stability
المشرفين على المادة: EC 3.1.1.3 (Lipase)
0 (Enzymes, Immobilized)
0 (Fungal Proteins)
9012-36-6 (Sepharose)
EC 3.1.1.3 (lipase B, Candida antarctica)
0 (Propionates)
0 (Solvents)
SCR Organism: Diutina rugosa
تواريخ الأحداث: Date Created: 20240525 Date Completed: 20240525 Latest Revision: 20240527
رمز التحديث: 20240527
مُعرف محوري في PubMed: PMC11121684
DOI: 10.3390/ijms25105084
PMID: 38791124
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms25105084