Abagnale, Maria (2018) Development of Microstructured Bioreactors for Green Chemistry Applications. [Tesi di dottorato]

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Item Type: Tesi di dottorato
Resource language: English
Title: Development of Microstructured Bioreactors for Green Chemistry Applications
Creators:
CreatorsEmail
Abagnale, Mariamaria.abagnale@unina.it
Date: 11 December 2018
Number of Pages: 151
Institution: Università degli Studi di Napoli Federico II
Department: Ingegneria Chimica, dei Materiali e della Produzione Industriale
Dottorato: Ingegneria dei prodotti e dei processi industriali
Ciclo di dottorato: 31
Coordinatore del Corso di dottorato:
nomeemail
Mensitieri, Giuseppemensitie@unina.it
Tutor:
nomeemail
Pirozzi, DomenicoUNSPECIFIED
Date: 11 December 2018
Number of Pages: 151
Keywords: Biocatalysis, Enzyme Immobilization, Enzyme stability, Sol-Gel technology, Microstructured Bioreactors
Settori scientifico-disciplinari del MIUR: Area 09 - Ingegneria industriale e dell'informazione > ING-IND/24 - Principi di ingegneria chimica
Date Deposited: 07 Jan 2019 23:37
Last Modified: 16 Jun 2020 10:22
URI: http://www.fedoa.unina.it/id/eprint/12584

Collection description

Future generations should be able to benefit from a previous responsible economic and social growth, triggered by a good management of the sources nowadays available for the industrial production. For decades by now, renewable sources have been a topic on the agenda overall the world, and the need to have eco-friendly processes has been a heartfelt matter, to cope with the continuous degradation, due to an improper administration of the environmental resources, which continues to affect our planet. For this reason, in each industrial field there is a sort of challenge to gain the greenness for its own processes, in order to positively answer to some general programmes, designed to preserve the environment from further negative changes. It is in this view that biocatalysis has made inroads in several industrial fields, but it is worthy to say that its whole employment is still far, because its widespread use in industry will require a proper conversion to achieve high space-time yield, to be competitive with the synthetic catalysis. The aim of this thesis is to explore the capacity, efficiency and productivity of enzymatic microstructured reactors, designed adopting the sol-gel technology as the enzyme immobilisation procedure, in order to offer the industries a tool to respond to some issues regarding catalytic processes. For this purpose, many industrially interesting enzymes have been immobilised, properly tuning some parameters, in order to achieve the best microenvironment for each one of them and to take advantages from their properties, overcoming some problems related to the use of free biocatalysts, especially as regards recycling and repeatability. The chosen enzymes for this research were a Lipase from Candida rugosa (CRL), a Xylanase from Thermomyces lanuginosus (TLX), a D-phenylglycine aminotransferase, isolated from Pseudomonas stutzeri ST-201 (D-PhgAT). All these enzymes are of great industrial interest, as they offer alternative methods for the synthesis of high value-added products. These methods require mild operative conditions, whereas the conventional chemical routes frequently prescribe severe values of pH and temperature. As a consequence, the enzyme processes can significantly increase the yield and the purity of refined products, often highly required. The industrial potential of these enzymes is well known: • a lipase can catalyse biotransformations of triglycerides and their derivates, in order to gain high added value products, such as natural surfactants, fats, natural flavours, but it can be also employed in the biosensors field, e.g. for triglycerides determination; • a xylanase is able to catalyse the hydrolysis of glycosidic bonds within the xylan, that is a polysaccharide of the family of hemicelluloses, which complete degradation brings to the formation of smaller molecules, known as xylo-oligosaccharides (XOS), which can be considered as prebiotics; • a D-phenylglycine aminotransferase can be used in transamination reactions between an amino acid and an α-ketoacid, for the synthesis of certain amino acids very difficult to obtain via synthetic route, and highly demanded especially in the pharmaceutical field. The catalytic performance of each one of the considered enzymes has been optimized with reference to specifically selected industrial processes. In particular, the sol-gel immobilization procedure has been modulated for every enzyme as regards the following aspects: - choice of precursors, focusing the attention on the silane oxides; - hydrolysis/condensation relative rate, acting on main parameters affecting the process kinetics; - choice of the final treatment, exploring the effect of a total desiccation versus lyophilisation, to obtain a porous material. Another issue addressed in this thesis is the optimization of the reactive operating conditions for the various analysed catalytic processes, both in batch and in continuous mode; in this view, a continuous reactor scheme design was accomplished on a lab scale for each enzymatic system.

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