دورية أكاديمية
أعرض في EDS

Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles.

التفاصيل البيبلوغرافية
العنوان: Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles.
المؤلفون: Melo RLF; Departamento de Engenharia Metalúrgica e de Materiais, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60440-554, Brazil; Grupo de Química de Materiais Avançados (GQMat), Departamento de Química Analítica e Físico-Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60451-970, Brazil., Freire TM; Grupo de Química de Materiais Avançados (GQMat), Departamento de Química Analítica e Físico-Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60451-970, Brazil., Valério RBR; Grupo de Química de Materiais Avançados (GQMat), Departamento de Química Analítica e Físico-Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60451-970, Brazil., Neto FS; Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60455-760, Brazil., de Castro Bizerra V; Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Campus das Auroras, Redenção, CE CEP 62790-970, Brazil., Fernandes BCC; Departamento de Agronomia e Ciência Vegetais, Universidade Federal Rural do Semi-Árido, Campus Mossoró, Mossoró, RN CEP 59625-900, Brazil., de Sousa Junior PG; Departamento de Química Orgânica e Inorgânica, Centro de Ciências, Universidade Federal do Ceará, Campus Pici, Fortaleza, CE CEP 60455760, Brazil., da Fonseca AM; Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Campus das Auroras, Redenção, CE CEP 62790-970, Brazil., Soares JM; Departamento de Física, Universidade do Estado do Rio Grande do Norte, Campus Mossoró, Mossoró, RN CEP 59610-090, Brazil., Fechine PBA; Grupo de Química de Materiais Avançados (GQMat), Departamento de Química Analítica e Físico-Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60451-970, Brazil., Dos Santos JCS; Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Campus das Auroras, Redenção, CE CEP 62790-970, Brazil. Electronic address: jcs@unilab.edu.br.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2024 Apr; Vol. 264 (Pt 2), pp. 130730. Date of Electronic Publication: 2024 Mar 10.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Lipase*/chemistry , Magnetite Nanoparticles*, Enzymes, Immobilized/chemistry ; Plant Oils/chemistry ; Esterification ; Enzyme Stability
مستخلص: Magnetic nanoparticles were functionalized with polyethylenimine (PEI) and activated with epoxy. This support was used to immobilize Lipase (Eversa® Transform 2.0) (EVS), optimization using the Taguchi method. XRF, SEM, TEM, XRD, FTIR, TGA, and VSM performed the characterizations. The optimal conditions were immobilization yield (I.Y.) of 95.04 ± 0.79 %, time of 15 h, ionic load of 95 mM, protein load of 5 mg/g, and temperature of 25 °C. The maximum loading capacity was 25 mg/g, and its stability in 60 days of storage showed a negligible loss of only 9.53 % of its activity. The biocatalyst demonstrated better stability at varying temperatures than free EVS, maintaining 28 % of its activity at 70 °C. It was feasible to esterify free fatty acids (FFA) from babassu oil with the best reaction of 97.91 % and ten cycles having an efficiency above 50 %. The esterification of produced biolubricant was confirmed by NMR, and it displayed kinematic viscosity and density of 6.052 mm 2 /s and 0.832 g/cm 3 , respectively, at 40 °C. The in-silico study showed a binding affinity of -5.8 kcal/mol between EVS and oleic acid, suggesting a stable substrate-lipase combination suitable for esterification.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: Babassu oil; Biofuels; Eversa lipase; Heterofunctional immobilization
المشرفين على المادة: EC 3.1.1.3 (Lipase)
0 (Enzymes, Immobilized)
0 (Magnetite Nanoparticles)
0 (Plant Oils)
تواريخ الأحداث: Date Created: 20240310 Date Completed: 20240410 Latest Revision: 20240410
رمز التحديث: 20240410
DOI: 10.1016/j.ijbiomac.2024.130730
PMID: 38462111
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2024.130730