RESUMEN
Crude olive pomace oil (OPO) is a by-product of olive oil extraction. In this study, low-calorie structured triacylglycerols (TAGs) were produced by acidolysis of crude OPO with medium-chain fatty acids (caprylic, C8:0; capric, C10:0) or interesterification with their ethyl ester forms (C8EE, C10EE). These new TAGs present long-chain fatty acids (L) at position sn-2 and medium-chain fatty acids (M) at positions sn-1,3 (MLM). Crude OPO exhibited a high acidity (12.05-28.75% free fatty acids), and high contents of chlorophylls and oxidation products. Reactions were carried out continuously in a packed-bed bioreactor for 70 h, using sn-1,3 regioselective commercial immobilized lipases (Thermomyces lanuginosus lipase, Lipozyme TL IM; and Rhizomucor miehei lipase, Lipozyme RM IM), in solvent-free media at 40 °C. Lipozyme RM IM presented a higher affinity for C10:0 and C10EE. Lipozyme TL IM preferred C10:0 over C8:0 but C8EE over C10EE. Both biocatalysts showed a high activity and operational stability and were not affected by OPO acidity. The New TAG yields ranged 30-60 and the specific productivity ranged 0.96-1.87 g NewTAG/h.g biocatalyst. Lipozyme RM IM cost is more than seven-fold the Lipozyme TL IM cost. Therefore, using Lipozyme TL IM and crude acidic OPO in a continuous bioreactor will contribute to process sustainability for structured lipid production by lowering the cost of the biocatalyst and avoiding oil refining.
Asunto(s)
Dietética , Olea , Olea/metabolismo , Aceites de Plantas , Grasas de la Dieta , Triglicéridos , Ácidos Grasos , Aceite de Oliva , Lipasa/metabolismo , Esterificación , Enzimas Inmovilizadas/metabolismoRESUMEN
In this study, crude oils extracted from spent coffee grounds (SCG) and olive pomace (OP) were used as raw-material to synthesize low-calorie triacylglycerols, either by acidolysis with capric acid, or by interesterification with ethyl caprate, in solvent-free media, catalyzed by sn-1,3 regioselective lipases. The Rhizopus oryzae lipase (ROL) was immobilized in magnetite nanoparticles (MNP-ROL) and tested as novel biocatalyst. MNP-ROL performance was compared with that of the commercial immobilized Thermomyces lanuginosus lipase (Lipozyme TL IM). For both oils, Lipozyme TL IM preferred interesterification over acidolysis. MNP-ROL catalyzed reactions were faster and acidolysis was preferred with yields of c.a. 50% new triacylglycerols after 3 h acidolysis of OP or SCG oils. MNP-ROL was very stable following the Sadana deactivation model with half-lives of 163 h and 220 h when reused in batch acidolysis and interesterification of OP oil, respectively.
Asunto(s)
Nanopartículas de Magnetita , Petróleo , Catálisis , Café , Enzimas Inmovilizadas , Esterificación , Lipasa , Lípidos , Aceite de OlivaRESUMEN
In this chapter, some examples of laboratory protocols to produce functional structured lipids, namely, human milk fat substitutes, dietetic triacylglycerols, and interesterified fat blends with improved nutritional and rheological properties, catalyzed either by immobilized commercial or noncommercial lipase preparations, are presented. In addition to batch synthesis, the continuous production in packed- or fluidized-bed bioreactors is addressed, as well as the evaluation of operational stability of the biocatalysts used (either in batch reuses or in continuous mode).
Asunto(s)
Lipasa/química , Lípidos/síntesis química , Biología Sintética , Catálisis , Grasas de la Dieta/síntesis química , Esterificación , Ácidos Grasos/química , Humanos , Técnicas In Vitro , Lípidos/química , Leche Humana/química , Biología Sintética/métodosRESUMEN
This study explores the potential for enhancing the production of ethyl lactate (EL), a green solvent, through enzymatic esterification. Different solvents were compared as organic media for conversion of lactate and ethanol into EL, catalyzed by Novozym 435. Chloroform and hexane were the most effective in low acid concentrations (0.01-0.1M) exhibiting maximum EL yields of 88% and 75% respectively. The yield of EL improved as the solvent's LogP increased up to a value of 2. Non-commercial immobilized biocatalysts consisting heterologous Rhizopous oryzae (rROL) and Candida rugosa (CRL) lipases immobilized on hydrophobic supports were compared to commercial biocatalysts clarifying that Novozym 435 and Lipozyme RM IM could be efficiently applied. Operational stability tests were conducted using Novozym 435, which retained higher activity in chloroform as compared to hexane. Although non-commercial biocatalysts were not competitive in esterification, they exhibited significant activity towards hydrolysis constituting a valuable alternative to higher-cost options.