Influence of the operating conditions on lipase-catalysed synthesis of ricinoleic acid estolides in solvent-free systems

Bódalo, A.; Bastida, Jaume; Máximo, M.F.; Montiel, M.C.; Murcia, M.D.; Ortega, S.

doi:10.1016/j.bej.2008.12.007

Cited by 34 publications

(48 citation statements)

References 16 publications

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“…3 . The AV of the estolide 56.9 2.9 mg KOH/g was lower than that reported previously 65 mg KOH/g 1 and reaction time 10 h was significant shorter than those 48 h of lipasecatalyzed reactions 1,7 . These results were attributed to the strong acidity of BSO 3 HMIM TS 21,22 , which can provide more catalytic activity sites for the esterification.…”

Section: Effect Of Different Functional Ilscontrasting

confidence: 46%

Synthesis of Ricinoleic Acid Estolides by the Esterification of Ricinoleic Acids Using Functional Acid Ionic Liquids as Catalysts

Wang

Sun

2017

J. Oleo Sci.

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Section: Effect Of Different Functional Ilscontrasting

confidence: 46%

Synthesis of Ricinoleic Acid Estolides by the Esterification of Ricinoleic Acids Using Functional Acid Ionic Liquids as Catalysts

Wang

Sun

2017

J. Oleo Sci.

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“…As previously discussed, water plays a fundamental role in the interesterification reactions, since it is responsible for the equilibrium between hydrolysis and esterification. In addition, water is required to maintain the catalytic function of these enzymes since it contributes, either directly or indirectly, to all the interactions that maintain the conformation of the active site, and consequently, the Assessing the reaction conditions to mediate the milkfat-soybean oil enzymatic interesterification Paula, A. V. et al catalytic function of these biocatalysts (BODALO et al, 2009). It is probable that the amount of water present in the reaction medium was not sufficient to maintain the catalytic activity of the lipase when the biocatalyst moisture content was only 5%.…”

Section: Resultsmentioning

confidence: 99%

Assessing the reaction conditions to mediate the milkfat-soybean oil enzymatic interesterification

Paula

Nunes

Castro

et al. 2016

Braz. J. Food Technol.

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This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Assessing the reaction conditions to mediate the milkfat-soybean oil enzymatic interesterification Determinação das condições reacionais para mediar a interesterificação enzimática da gordura do leite e do óleo de soja SummaryA food grade lipase from Rhizopus oryzae immobilized on a hybrid polysiloxane-polyvinyl alcohol matrix (SiO 2 -PVA) was used as the biocatalyst to mediate the interesterification reactions of a blend containing 65% milkfat and 35% soybean oil. All the reactions occurred in an inert nitrogen atmosphere in cylindrical glass reactors (80 mL) with 40 g of the milkfat-soybean oil blend. The influence of the following variables was evaluated: biocatalyst loading (250-1500 activity units per gram of blend), biocatalyst moisture content (5-20%), temperature (45-60 °C) and incubation time (2-48 h). The reactions were monitored by determining the free fatty acid content, triacylglycerol (TAGs) composition in carbon species, and the consistency of the interesterified (IE) products. The reaction conditions were set based on the parameters that provided a high interesterification yield and good consistency of the final product within the ideal range (200 to 800 gf cm -2 ). Hence the best results were obtained using a biocatalyst loading of 500 U g -1 of blend with 10% moisture content at 45 °C for 4 h. Under these conditions the consistency of the interesterified product was 539.7 ± 38 gf cm -2 . The results demonstrated the potential of the immobilized lipase to alter the TAGs profile of the milkfat-soybean oil blend, allowing for the production of structured lipids.Keywords: Rhizopus oryzae lipase; Milkfat; Soybean oil; Interesterification. ResumoLipase de grau alimentício de Rhizopus oryzae, imobilizada em uma matriz híbrida de polissiloxano-polivinilálcool (SiO 2 -PVA), foi usada como biocatalisador para mediar reações de interesterificação de uma mistura contendo 65% de gordura de leite e 35% de óleo de soja. Todas as reações ocorreram sob atmosfera inerte de nitrogênio, em reatores de vidro cilíndricos (80 mL) com 40 g da mistura. Avaliou-se a influência das seguintes variáveis: carregamento de biocatalisador (250-1.500 unidades de atividade por grama de mistura), umidade do biocatalisador (5-20%), temperatura (45-60 °C) e tempo de incubação (2-48 h). O progresso das reações foi monitorado pela determinação do conteúdo de ácidos graxos livres, da composição em triacilgliceróis (TAGs) em espécies de carbono e da consistência de produtos interesterificados (IE). As condições reacionais foram estabelecidas com base nos parâmetros que proporcionaram alto grau de interesterificação e consistência do produto final dentro da faixa ideal (200 a 800 gf cm -2 ). Neste contexto, os melhores resultados foram obtidos utilizando-se 500 U de biocatalisador por grama de mistura, com 10% de...

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“…The differences between these enzymatic preparations lie not only in the lipase immobilized, the technique of immobilization and the carrier used, but also in their prices, being CalB immo Plus 2.5‐3 times more expensive than Lipozyme ® RM IM. According to the authors previous experience, the process has been performed under vacuum conditions, as pushing the reaction equilibrium towards the ester synthesis by eliminating the water present in reaction media significantly increases the final conversion ,…”

Section: Introductionmentioning

confidence: 99%

One‐Step Solvent‐Free Production of a Spermaceti Analogue Using Commercial Immobilized Lipases

et al. 2018

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The enzymatic synthesis of fine chemicals is a promising approach to overcome the major problems of the traditional chemical routes and implement eco‐friendly and low energy consuming industrial processes. This work introduces for the first time the one‐step production of an analogue of the sperm whale's spermaceti in a vacuum, solvent‐free system. With the aim of easing the industrial feasibility of the process, two commercial biocatalysts with appropriate technical properties were tested. Results pointed out that under optimal conditions, both commercial immobilized derivatives (Lipozyme® RM IM and CalB immo Plus) gave excellent results as they can be reused up to 15 batches without a noticeable loss of their activity, obtaining conversions of ∼98% in two hours. This green and sustainable process might be economically competitive and leads to a product that meets the all specifications required for its cosmetic use and that can be labeled as “natural”, increasing its added value.

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Influence of the operating conditions on lipase-catalysed synthesis of ricinoleic acid estolides in solvent-free systems

Cited by 34 publications

References 16 publications

Synthesis of Ricinoleic Acid Estolides by the Esterification of Ricinoleic Acids Using Functional Acid Ionic Liquids as Catalysts

Synthesis of Ricinoleic Acid Estolides by the Esterification of Ricinoleic Acids Using Functional Acid Ionic Liquids as Catalysts

Assessing the reaction conditions to mediate the milkfat-soybean oil enzymatic interesterification

One‐Step Solvent‐Free Production of a Spermaceti Analogue Using Commercial Immobilized Lipases

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