Enzymes are currently used in a wide variety of industries and some of the most exploited are the lipases thanks to their unique versatility [1]. In nature they principally hydrolyze triglycerides, but they are also able to catalyze in vitro esterification, acidolysis, interesterificaton, transesterification, and aminolysis, together with a collection of the so-called promiscuous reactions [2]. However, how every other enzyme, lipases have a low stability and immobilization procedures are often applied to enhance their performances. The most common immobilization methodologies are covalent immobilization, physical adsorption, cross-linking, encapsulation, and entrapment on both synthetic and natural derived materials [3]. Although synthetic materials have many advantages, they are difficult to obtain and require higher additional costs. On the other hand, material derived from natural sources, like spent coffee grounds (SCG), have favorable physical-chemical characteristics and are also largely available and inexpensive. Coffee, in particular, had an estimated production of over 10 billion kg per year in 2020 [4] and is responsible for generating large quantities of residues that may represent a great pollution hazard if discharged into the environment. Therefore, the aim of this study is focused on the ideation of a suitable carrier for Candida Rugosa Lipase (CRL) from SCG. With this purpose SCG was pretreated in different ways to assure the best characteristics for each methodology of immobilization. The materials were characterized by SEM, IR, and elemental analysis. Subsequentially four different kinds of immobilization methods were evaluated: (i) adsorption, (ii) crosslinking, (iii) covalent binding after periodate oxidation of the support and (vi) covalent binding after activation of the support with glutaraldehyde (GLU). The optimal immobilization conditions were determined on the base of yield, efficiency, and recovery. [1] A. Houde, A. Kademi, D. Leblanc, Applied Biochemistry and Biotechnology 118 (2004) 155–170. [2] C. Ortiz, M.L. Ferreira, O. Barbosa, J.C.S. Dos Santos, R.C. Rodrigues, Á. Berenguer-Murcia, L.E. Briand, R. Fernandez-Lafuente, Catalysis Science & Technology 9 (2019) 2380–2420. [3] B. Thangaraj, P.R. Solomon, ChemBioEng Reviews 6 (2019) 167–194. [4] International Coffee Organization (2022).
Comparison of lipase immobilization methods on spent coffee grounds (SCG) supports / Chiappini, Viviana; Girelli, Anna Maria. - (2022). (Intervento presentato al convegno XXIX Congresso della Divisione di Chimica Analitica - La Chimica Analitica per un futuro verde e sostenibile tenutosi a Milazzo (ME)).
Comparison of lipase immobilization methods on spent coffee grounds (SCG) supports
Viviana, Chiappini
Formal Analysis
;Anna Maria, Girelli
2022
Abstract
Enzymes are currently used in a wide variety of industries and some of the most exploited are the lipases thanks to their unique versatility [1]. In nature they principally hydrolyze triglycerides, but they are also able to catalyze in vitro esterification, acidolysis, interesterificaton, transesterification, and aminolysis, together with a collection of the so-called promiscuous reactions [2]. However, how every other enzyme, lipases have a low stability and immobilization procedures are often applied to enhance their performances. The most common immobilization methodologies are covalent immobilization, physical adsorption, cross-linking, encapsulation, and entrapment on both synthetic and natural derived materials [3]. Although synthetic materials have many advantages, they are difficult to obtain and require higher additional costs. On the other hand, material derived from natural sources, like spent coffee grounds (SCG), have favorable physical-chemical characteristics and are also largely available and inexpensive. Coffee, in particular, had an estimated production of over 10 billion kg per year in 2020 [4] and is responsible for generating large quantities of residues that may represent a great pollution hazard if discharged into the environment. Therefore, the aim of this study is focused on the ideation of a suitable carrier for Candida Rugosa Lipase (CRL) from SCG. With this purpose SCG was pretreated in different ways to assure the best characteristics for each methodology of immobilization. The materials were characterized by SEM, IR, and elemental analysis. Subsequentially four different kinds of immobilization methods were evaluated: (i) adsorption, (ii) crosslinking, (iii) covalent binding after periodate oxidation of the support and (vi) covalent binding after activation of the support with glutaraldehyde (GLU). The optimal immobilization conditions were determined on the base of yield, efficiency, and recovery. [1] A. Houde, A. Kademi, D. Leblanc, Applied Biochemistry and Biotechnology 118 (2004) 155–170. [2] C. Ortiz, M.L. Ferreira, O. Barbosa, J.C.S. Dos Santos, R.C. Rodrigues, Á. Berenguer-Murcia, L.E. Briand, R. Fernandez-Lafuente, Catalysis Science & Technology 9 (2019) 2380–2420. [3] B. Thangaraj, P.R. Solomon, ChemBioEng Reviews 6 (2019) 167–194. [4] International Coffee Organization (2022).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
