Giacobelli, Valerio Guido (2017) Wild-Type and mutated laccases for a green industry. [Tesi di dottorato]

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Item Type: Tesi di dottorato
Lingua: English
Title: Wild-Type and mutated laccases for a green industry
Creators:
CreatorsEmail
Giacobelli, Valerio Guidovalerioguido.giacobelli@unina.it
Date: 7 April 2017
Number of Pages: 105
Institution: Università degli Studi di Napoli Federico II
Department: Scienze Chimiche
Scuola di dottorato: Biotecnologie
Dottorato: Biotecnologie
Ciclo di dottorato: 29
Coordinatore del Corso di dottorato:
nomeemail
Sannia, Giovannisannia@unina.it
Tutor:
nomeemail
Sannia, GiovanniUNSPECIFIED
Date: 7 April 2017
Number of Pages: 105
Uncontrolled Keywords: Laccase site-specific mutagenesis industrial application dye
Settori scientifico-disciplinari del MIUR: Area 05 - Scienze biologiche > BIO/11 - Biologia molecolare
Date Deposited: 18 Apr 2017 13:09
Last Modified: 08 Mar 2018 08:46
URI: http://www.fedoa.unina.it/id/eprint/11506
DOI: 10.6093/UNINA/FEDOA/11506

Abstract

In the frame of white biotechnology, enzymes attract an enormous attention both for their potential and for the recent social and economical interest in green chemistry. Thanks to the improved knowledge of production biochemistry, fermentation processes, and recovery methods, an increasing number of enzymes can be affordably produced. The majority of currently used industrial enzymes are the hydrolytic ones, being used for the degradation of various natural substances. Also, various oxidative enzymes, primarily laccases are used in industries such as the starch, textile, detergent and baking industries, and they represent a second important group of enzymes. This project has been focused on the recombinant expression of the industrially attractive laccase POXA1b from Pleurotus ostreatus in Pichia pastoris and on exploiting its industrial application in order to substitute some chemical industrial processes with a better eco-friendly ones. An economical analysis of the recombinant POXA1b laccase production process, in terms of productivity and cost has been evaluated. Furthermore, computational analysis and site-specific mutagenesis of the POXA1b were performed to increase the enzymatic performances towards selected substrates. A POXA1b laccase immobilization process was optimized by statistic methods (Response Surface Methodology) in order to increment the operational stability of the enzyme in specific processes. Applications of the recombinant enzyme were then developed: (i) reduction of the phenol contents inside the fruit juices by immobilized laccase POXA1b; (ii) synthesis of a new eco-friendly dyes for the staining of different textile materials (nylon, cotton and wool) and (iii) synthesis of a new eco-friendly dye for proteins visualization on the polyacrilamide gels; (iv) cotton fiber functionalization with an anti-adhesive and anti-oxidant dye polymer.

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