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      Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils

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          Abstract

          Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized by covalent binding with epichlorohydrin without (203%) and with PIL (250%), was assessed by the following the hydrolysis reaction of olive oil and characterized biochemically (Michaelis–Menten constant, optimum pH and temperature, and operational stability). Further, the potential transesterification activity for three substrates: sunflower, soybean, and colza oils, was also determined, achieving a conversion of ethyl esters between 70 and 98%. The supports and the immobilized lipase systems were characterized using Fourier transform infrared spectra (FTIR), scanning electron microscopy (SEM), elemental analysis, and thermogravimetric (TG) analysis.

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          Enzyme immobilisation in biocatalysis: why, what and how.

          In this tutorial review, an overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented. The importance of biocatalysis in the context of green and sustainable chemicals manufacture is discussed and the necessity for immobilisation of enzymes as a key enabling technology for practical and commercial viability is emphasised. The underlying reasons for immobilisation are the need to improve the stability and recyclability of the biocatalyst compared to the free enzyme. The lower risk of product contamination with enzyme residues and low or no allergenicity are further advantages of immobilised enzymes. Methods for immobilisation are divided into three categories: adsorption on a carrier (support), encapsulation in a carrier, and cross-linking (carrier-free). General considerations regarding immobilisation, regardless of the method used, are immobilisation yield, immobilisation efficiency, activity recovery, enzyme loading (wt% in the biocatalyst) and the physical properties, e.g. particle size and density, hydrophobicity and mechanical robustness of the immobilisate, i.e. the immobilised enzyme as a whole (enzyme + support). The choice of immobilisate is also strongly dependent on the reactor configuration used, e.g. stirred tank, fixed bed, fluidised bed, and the mode of downstream processing. Emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).
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            Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance

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              Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.

              Glutaraldehyde possesses unique characteristics that render it one of the most effective protein crosslinking reagents. It can be present in at least 13 different forms depending on solution conditions such as pH, concentration, temperature, etc. Substantial literature is found concerning the use of glutaraldehyde for protein immobilization, yet there is no agreement about the main reactive species that participates in the crosslinking process because monomeric and polymeric forms are in equilibrium. Glutaraldehyde may react with proteins by several means such as aldol condensation or Michael-type addition, and we show here 8 different reactions for various aqueous forms of this reagent. As a result of these discrepancies and the unique characteristics of each enzyme, crosslinking procedures using glutaraldehyde are largely developed through empirical observation. The choice of the enzyme-glutaraldehyde ratio, as well as their final concentration, is critical because insolubilization of the enzyme must result in minimal distortion of its structure in order to retain catalytic activity. The purpose of this paper is to give an overview of glutaraldehyde as a crosslinking reagent by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                21 June 2018
                July 2018
                : 19
                : 7
                Affiliations
                [1 ]Institute of Technology and Research, Avenida Murilo Dantas 300, Aracaju 49032-490, Sergipe, Brazil; nayara.eng@ 123456hotmail.com (N.B.C.); brunabtv@ 123456hotmail.com (B.T.V.); andinhobarbosa@ 123456hotmail.com (A.S.B.); matheus.pereira@ 123456ua.pt (M.M.P.); aslima2001@ 123456yahoo.com.br (A.S.L.)
                [2 ]Postgraduate in Process Engineering, Tiradentes University, Avenida Murilo Dantas 300, Aracaju 49032-490, Sergipe, Brazil
                [3 ]Department of Chemical Engineering, Federal University of Bahia, Rua Prof. Aristides Novis, 02, Federação, Salvador 40210-630, Bahia, Brazil; silvana@ 123456ufba.br
                [4 ]Department of Chemistry, Federal University of Sergipe, Av. Marechal Rondon, s/n, Jd. Rosa Elze, São Cristóvão 49100-000, Sergipe, Brazil; lisiane_santos_freitas@ 123456yahoo.com.br
                Author notes
                [* ]Correspondence: cleide.soares@ 123456pq.cnpq.br ; Tel.: +55-79-32182115
                Article
                ijms-19-01829
                10.3390/ijms19071829
                6073416
                29933608
                © 2018 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

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