دورية أكاديمية

Deciphering the immobilization of lipases on hydrophobic wrinkled silica nanoparticles.

التفاصيل البيبلوغرافية
العنوان: Deciphering the immobilization of lipases on hydrophobic wrinkled silica nanoparticles.
المؤلفون: Pota G; Department of Chemical, Materials and Production Engineering, University of Naples Federico II, Piazzale Tecchio 80, 80125 Fuorigrotta, Naples, Italy., Andrés-Sanz D; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), 20014 Donostia, San Sebastián, Spain., Gallego M; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), 20014 Donostia, San Sebastián, Spain., Vitiello G; Department of Chemical, Materials and Production Engineering, University of Naples Federico II, Piazzale Tecchio 80, 80125 Fuorigrotta, Naples, Italy; CSGI, Center for Colloid and Surface Science, Sesto Fiorentino, FI, Italy., López-Gallego F; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), 20014 Donostia, San Sebastián, Spain; IKERBASQUE, Basque Foundation for Science, 48013 Bilbao, Spain. Electronic address: flopez@cicbiomagune.es., Costantini A; Department of Chemical, Materials and Production Engineering, University of Naples Federico II, Piazzale Tecchio 80, 80125 Fuorigrotta, Naples, Italy. Electronic address: anicosta@unina.it., Califano V; Institute of Science and Technology for Sustainable Energy and Mobility (STEMS), National Research Council of Italy (CNR), Viale Marconi 4, 80125 Naples, Italy.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2024 May; Vol. 266 (Pt 1), pp. 131022. Date of Electronic Publication: 2024 Mar 22.
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: Enzymes, Immobilized*/chemistry , Enzymes, Immobilized*/metabolism , Lipase*/chemistry , Lipase*/metabolism , Silicon Dioxide*/chemistry , Hydrophobic and Hydrophilic Interactions* , Nanoparticles*/chemistry , Enzyme Stability*, Adsorption ; Kinetics ; Rhizomucor/enzymology ; Fungal Proteins/chemistry ; Hydrolysis ; Temperature
مستخلص: In this work, the adsorption of Candida antarctica B (CALB) and Rhizomucor miehei (RML) lipases into hydrophobic wrinkled silica nanoparticles (WSNs) is investigated. WSNs are hydrophobized by chemical vapor deposition. Both proteins are homogeneously distributed inside the pores of the nanoparticles, as confirmed by Transmission Electron Microscopy and Energy Dispersive X-ray measurements. The maximum enzyme load of CALB is twice that obtained for RML. Fourier Transform Infrared Spectroscopy confirms the preservation of the enzyme secondary structure after immobilization for both enzymes. Adsorption isotherms fit to a Langmuir model, resulting in a binding constant (K L ) for RML 4.5-fold higher than that for CALB, indicating stronger binding for the former. Kinetic analysis reveals a positive correlation between enzyme load and RML activity unlike CALB where activity decreases along the enzyme load increases. Immobilization allows for enhancing the thermal stability of both lipases. Finally, CALB outperforms RML in the hydrolysis of ethyl-3-hydroxybutyrate. However, immobilized CALB yielded 20 % less 3-HBA than free lipase, while immobilized RML increases 3-fold the 3-HBA yield when compared with the free enzyme. The improved performance of immobilized RML can be explained due to the interfacial hyperactivation undergone by this lipase when immobilized on the superhydrophobic surface of WSNs.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
(Copyright © 2024. Published by Elsevier B.V.)
فهرسة مساهمة: Keywords: Hydrophobicity; Immobilization; Interfacial activation; Lipase; Mesoporous silica nanoparticles
المشرفين على المادة: 0 (Enzymes, Immobilized)
EC 3.1.1.3 (Lipase)
7631-86-9 (Silicon Dioxide)
0 (Fungal Proteins)
EC 3.1.1.3 (lipase B, Candida antarctica)
تواريخ الأحداث: Date Created: 20240324 Date Completed: 20240430 Latest Revision: 20240430
رمز التحديث: 20240501
DOI: 10.1016/j.ijbiomac.2024.131022
PMID: 38522688
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2024.131022