Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability

Surface adsorption is a convenient and readily available method for immobilizing enzymes on metal-organic frameworks (MOFs). Metal-organic framework-5 (MOF-5), isoreticular metal-organic frameworks-3 (IRMOF-3), and multivariate analysis of MOF-5/IRMOF-3 (MMI) with a half-amino group (-NH2) were prep...

Full description

Bibliographic Details
Published in:Engineering Microbiology
Main Authors: Zeynab Rangraz, Mostafa M. Amini, Zohreh Habibi
Format: Article
Language:English
Published: Elsevier 2024-12-01
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2667370324000389
_version_ 1849568089182568448
author Zeynab Rangraz
Mostafa M. Amini
Zohreh Habibi
author_facet Zeynab Rangraz
Mostafa M. Amini
Zohreh Habibi
author_sort Zeynab Rangraz
collection DOAJ
container_title Engineering Microbiology
description Surface adsorption is a convenient and readily available method for immobilizing enzymes on metal-organic frameworks (MOFs). Metal-organic framework-5 (MOF-5), isoreticular metal-organic frameworks-3 (IRMOF-3), and multivariate analysis of MOF-5/IRMOF-3 (MMI) with a half-amino group (-NH2) were prepared in this study. Thermomyces lanuginosus lipase (TLL) was chosen as a commercially available enzyme for immobilization on the surfaces of these MOFs. Briefly, 1.5 mg of TLL was added to 10 mg of the MOFs, and after 24 h, 67, 74, and 88% of the TLL was immobilized on MOF-5, IRMOF-3, and MMI, respectively. Fourier transform infrared spectroscopy, X-ray diffraction, thermogravimetric analysis, scanning electron microscopy, energy-dispersive X-ray analysis, and Brunauer–Emmett–Teller analysis were used to characterize the resulting biocomposites. TLL@MOF-5, TLL@IRMOF-3, and TLL@MMI exhibited activities of 55, 75, and 110 U/mg, respectively. Investigation of the activity and stability of the prepared biocatalysts showed that TLL immobilized on MMI was 2.34-fold more active than free TLL. TLL@MMI exhibited high stability and activity even under harsh conditions. After 24 h of incubation in a mixture of 50% (v/v) MeOH, TLL@MMI retained 80% of its activity, whereas TLL@MOF-5 and free TLL lost 50 and 60% of their activities, respectively. TLL@MMI was used to synthesize 2-arylidenehydrazinyl-4-arylthiozole derivatives (91–98%) in a one-pot vessel by adding benzaldehydes, phenacyl bromides, and thiosemicarbazide to water. The efficiency of the 4a derivative with free TLL was 43%, whereas that with TLL@MMI was 98%.
format Article
id doaj-art-3e4ea3d8171d4daba8ce329bfa1fb4d6
institution Directory of Open Access Journals
issn 2667-3703
language English
publishDate 2024-12-01
publisher Elsevier
record_format Article
spelling doaj-art-3e4ea3d8171d4daba8ce329bfa1fb4d62025-08-20T02:32:20ZengElsevierEngineering Microbiology2667-37032024-12-014410017610.1016/j.engmic.2024.100176Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stabilityZeynab Rangraz0Mostafa M. Amini1Zohreh Habibi2Department of Organic Chemistry, Faculty of Chemistry, Shahid Beheshti University, G.C., Tehran, IranDepartment of Inorganic Chemistry, Faculty of Chemistry, Shahid Beheshti University, G.C., Tehran, IranDepartment of Organic Chemistry, Faculty of Chemistry, Shahid Beheshti University, G.C., Tehran, Iran; Corresponding author.Surface adsorption is a convenient and readily available method for immobilizing enzymes on metal-organic frameworks (MOFs). Metal-organic framework-5 (MOF-5), isoreticular metal-organic frameworks-3 (IRMOF-3), and multivariate analysis of MOF-5/IRMOF-3 (MMI) with a half-amino group (-NH2) were prepared in this study. Thermomyces lanuginosus lipase (TLL) was chosen as a commercially available enzyme for immobilization on the surfaces of these MOFs. Briefly, 1.5 mg of TLL was added to 10 mg of the MOFs, and after 24 h, 67, 74, and 88% of the TLL was immobilized on MOF-5, IRMOF-3, and MMI, respectively. Fourier transform infrared spectroscopy, X-ray diffraction, thermogravimetric analysis, scanning electron microscopy, energy-dispersive X-ray analysis, and Brunauer–Emmett–Teller analysis were used to characterize the resulting biocomposites. TLL@MOF-5, TLL@IRMOF-3, and TLL@MMI exhibited activities of 55, 75, and 110 U/mg, respectively. Investigation of the activity and stability of the prepared biocatalysts showed that TLL immobilized on MMI was 2.34-fold more active than free TLL. TLL@MMI exhibited high stability and activity even under harsh conditions. After 24 h of incubation in a mixture of 50% (v/v) MeOH, TLL@MMI retained 80% of its activity, whereas TLL@MOF-5 and free TLL lost 50 and 60% of their activities, respectively. TLL@MMI was used to synthesize 2-arylidenehydrazinyl-4-arylthiozole derivatives (91–98%) in a one-pot vessel by adding benzaldehydes, phenacyl bromides, and thiosemicarbazide to water. The efficiency of the 4a derivative with free TLL was 43%, whereas that with TLL@MMI was 98%.http://www.sciencedirect.com/science/article/pii/S2667370324000389BiocatalystMOFEnzyme immobilizationLipaseThiazoles
spellingShingle Zeynab Rangraz
Mostafa M. Amini
Zohreh Habibi
Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
Biocatalyst
MOF
Enzyme immobilization
Lipase
Thiazoles
title Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
title_full Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
title_fullStr Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
title_full_unstemmed Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
title_short Immobilization of Thermomyces lanuginosus lipase on metal-organic frameworks and investigation of their catalytic properties and stability
title_sort immobilization of thermomyces lanuginosus lipase on metal organic frameworks and investigation of their catalytic properties and stability
topic Biocatalyst
MOF
Enzyme immobilization
Lipase
Thiazoles
url http://www.sciencedirect.com/science/article/pii/S2667370324000389
work_keys_str_mv AT zeynabrangraz immobilizationofthermomyceslanuginosuslipaseonmetalorganicframeworksandinvestigationoftheircatalyticpropertiesandstability
AT mostafamamini immobilizationofthermomyceslanuginosuslipaseonmetalorganicframeworksandinvestigationoftheircatalyticpropertiesandstability
AT zohrehhabibi immobilizationofthermomyceslanuginosuslipaseonmetalorganicframeworksandinvestigationoftheircatalyticpropertiesandstability