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Preparation and Comparison of Hydrolase‐Coated Plastics
Author(s) -
Spadoni Andreani Eugenio,
Magagnin Luca,
Secundo Francesco
Publication year - 2016
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201600377
Subject(s) - glutaraldehyde , lipase , immobilized enzyme , adsorption , polyethylene , chemistry , polypropylene , transesterification , surface modification , thermal stability , chromatography , enzyme , polymer chemistry , organic chemistry , catalysis
Polypropylene and polyethylene were coated with alpha‐Chymotrypsin (α‐CT) or subtilisin Carlsberg (SubC) or Burkholderia cepacia lipase (lipase BC) by different immobilization procedures, such as physical adsorption and covalent linking. This latter procedure was based on the chemical functionalization of the plastic surface by oxygen gas plasma treatment. Immobilization of the enzyme was carried out by using as cross‐linking agent i) glutaraldehyde (GA) or ii) N′‐diisopropylcarbodiimide (DIC) and N‐hydroxysuccinimide (NHS). The effects of duration of the plasma treatment and the type of the immobilization procedure on the transesterification activity of the enzyme were investigated. In general polypropylene resulted a better support than polyethylene. Moreover, α‐CT showed higher transesterification activity when immobilized with GA, while for SubC, DIC and NHS were better cross‐linking agents than GA. No activity was observed with these enzymes when immobilization was carried out by physical adsorption. On the contrary, lipase BC immobilized by physical adsorption was even more active than the free enzyme. Concerning thermal stability, immobilized SubC was less stable than the free enzyme. Overall, these results show that plastics endowed with biocatalytic properties could be obtained by simple immobilization protocols and that optimal immobilization conditions depend on the type of starting plastic, plasma treatment, cross‐linking method, and the nature of the enzyme.

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