Premium
Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements
Author(s) -
Naseri Maryam,
Pitzalis Federica,
Carucci Cristina,
Medda Luca,
Fotouhi Lida,
Magner Edmond,
Salis Andrea
Publication year - 2018
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201801293
Subject(s) - imidazolate , lipase , zeolitic imidazolate framework , laccase , chemistry , thermogravimetric analysis , biocatalysis , immobilized enzyme , nuclear chemistry , fourier transform infrared spectroscopy , catalysis , metal organic framework , adsorption , organic chemistry , chemical engineering , enzyme , ionic liquid , engineering
Abstract : Lipase ( Pseudomonas fluorescens ) and laccase ( Trametates versicolor ) were encapsulated on two zeolite imidazolate framework, ZIF‐8 and ZIF‐zni, materials using a one‐pot synthesis‐immobilization method in aqueous solution at room temperature. The synthesized immobilized biocatalysts (Lip@ZIF‐8, Lip@ZIF‐zni, Lac@ZIF‐8, and Lac@ZIF‐zni) were characterized by X‐ray diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The enzymatic activities of the four immobilized biocatalysts were characterized via the electrochemical detection of the substrates, p‐nitrophenyl butyrate and 2,2‐azinobis‐3‐ethylbenzthiazoline‐6‐sulfonic acid. For Lip@ZIF‐8 the specific activity was 91.9 U mg −1 and 123.1 U mg −1 for Lip@ZIF‐zni, while for Lac@ZIF‐8 and Lac@ZIF‐zni, the activity was 51 U mg −1 and 163 U mg −1 , respectively, confirming that laccase retains a higher level of activity when immobilized onto ZIF‐zni than on ZIF‐8. Lac@ZIF‐8 was the most stable system on storage (15 days at 5 °C), retaining 94 % of initial activity, while Lip@ZIF‐zni biocatalyst had the optimal level of reusability, retaining 40 % of initial activity after five reaction cycles.