Synthesis of cetyl ricinoleate catalyzed by immobilized Lipozyme® CalB lipase in a solvent-free system

Montiel, M.C.; Serrano, María del Carmen Martínez; Máximo, M.F.; Gómez, M.; Ortega‐Requena, Salvadora; Bastida, Jaume

doi:10.1016/j.cattod.2014.09.015

Cited by 18 publications

(12 citation statements)

References 17 publications

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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%

“…In this way, organic solvents, ionic liquids, and supercritical fluids have been employed, but either for the unnecessary severe operation conditions or for the risk of finding traces of the reaction media on the product, these methods are unsuitable for obtaining cosmetic or pharmaceutical compounds. Therefore, the enzymatic synthesis of these products can be faced with great success by operating under vacuum using a solvent‐free system, as it requires mild reaction conditions and purification steps are considerably reduced ,…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2018

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“…In addition, the use of enzymatic biotransformations in the cosmetic sector can contribute to achieving a "natural" designation [6], which has proved to be an increasingly effective marketing claim, as consumers often perceive natural cosmetics as safer, healthier, and more respectful with the environment [7]. In this sense, many examples of the lipase-based synthesis of emollient monoesters can be found in the literature [8][9][10][11], and even some processes have successfully been implemented at an industrial scale [12].…”

Section: Introductionmentioning

confidence: 99%

Green Production of a High-Value Branched-Chain Diester: Optimization Based on Operating Conditions and Economic and Sustainability Criteria

et al. 2023

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Branched-chain esters (BCEs) have found a large number of applications in cosmetics. Among them, neopentyl glycol dilaurate (NPGDL) stands out as an emollient, emulsifier, and skin-conditioning agent. This work presents the synthesis of NPGDL in a solvent-free medium using the two most common immobilized lipases: Novozym® 40086 (Rml) and Novozym® 435 (CalB). Results proved that the former biocatalyst has lower activity and certain temperature deactivation, although conversions ≥ 90% were obtained at 60 °C and 7.5% of catalyst. On the other hand, optimal reaction conditions for Novozym® 435 are 3.75% w/w of the immobilized derivative at 80 °C. Under optimal conditions, the process productivities were 0.105 and 0.169 kg NPGDL/L h, respectively. In order to select the best conditions for NPGDL production, studies on the reuse of the derivative and cost estimation have been performed. Economic study shows that biocatalytic processes can be competitive when lipases are reused for five cycles, yielding biocatalyst productivities of 56 and 122 kg NPGDL/kg biocatalyst using Novozym® 40086 and Novozym® 435, respectively. The final choice will be based on both economic and sustainability criteria. Green metric values using both biocatalysts are similar but the product obtained using Novozym® 40086 is 20% cheaper, making this alternative the best option.

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“…As a green catalyst, such as other enzymes, Candida antarctica lipase B (CALB, 3.1.1.3) has advantages when used as a catalyst, such as mild reaction conditions, chemo-and enantioselectivity, and high catalytic activity under mild reaction conditions. 7,8 As one of the most widely used enzymes in biocatalysis, CALB can efficiently catalyze hydrolysis, esterification, and transesterification reactions.…”

Section: Introductionmentioning

confidence: 99%

Application of magnetic field (MF) as an effective method to improve the activity of immobilized Candida antarctica lipase B (CALB)

Wang

Zhang

Yue

et al. 2022

Catal. Sci. Technol.

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Synthesis of cetyl ricinoleate catalyzed by immobilized Lipozyme® CalB lipase in a solvent-free system

Cited by 18 publications

References 17 publications

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

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

Green Production of a High-Value Branched-Chain Diester: Optimization Based on Operating Conditions and Economic and Sustainability Criteria

Application of magnetic field (MF) as an effective method to improve the activity of immobilized Candida antarctica lipase B (CALB)

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