Preliminary economic assessment: a valuable tool to establish biocatalytic process feasibility with an in-lab immobilized lipase.

BACKGROUND: Despite the interest that commercial lipases arouse, the number of 20 industrial applications is still very limited. Only high added value products such as 21 cosmetic ingredients that can simultaneously benefit of “green chemistry” and “natural” 22 labels of using biocatalysts can justify the final cost. In any case, process feasibility 23 economic assesment in the first project stages must be done to take decisions about its 24 industrial applicability. RESULTS: This work presents an economic study of cetyl esters 1 mixture production 2 process similar to natural spermaceti catalyzed by different in-lab immobilized lipase 3 derivatives to determine if they can compete, not only in catalytic properties (activity 4 and stability) but also in price, with the commercial ones. Among results highlight that 5 CALB lipase immobilized in Amberlite™ XAD™ 1180 whose direct total cost (1.20 6 €/g) is comparable to commercial lipases, is also effective in spermaceti biocatalytic 7 synthesis achieving, under optimal conditions, a 98 % of conversion in less than one.CONCLUSION: High conversion values and it reusability (at least 15 times) ,provides a product with a price (58 €/kg) similar to the obtained with the well known Novozym® 9 10 435 (56.5 €/kg). The future scale-up will allows to better study the process and gives a 11 more realistic product final price

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

green process has been performed for the synthesis of the emollient ester cetyl ricinoleate with a new immobilized derivative of Candida antarctica lipase B, which has been prepared by physical adsorption of Lipozyme® CalB L on a macroporous anionic exchange resin (Lewatit® MonoPlus MP 64). An immobilized CalB lipase with protein content over 30 mg/g has been obtained and it has been successfully used as biocatalyst to produce cetyl ricinoleate from esterification of ricinoleic acid with cetyl alcohol. Influence of amount of biocatalyst and temperature was studied in the open-air reactor, and optimal values could be fixed in 2 mg and 70ºC respectively. Biocatalyst storage stability study was developed in this reactor and it was showed the high storage stability of the immobilized derivative, because it keeps 100% of its enzymatic activity after eight months. Studies of recovery and reuse of the immobilized derivative were performed in the vacuum reactor, and it was proved the posibility of using the same biocatalyst in three consecutive reaction cycles without apparent loss of activity. Finally, the characterization of the cetyl ricinoleate obtained in the vacuum reactor demonstrated that the product obtained after only 3 or 4 hours of reaction meets manufacturers’ specifications

One-step solvent-free production of a spermaceti analogue using commercial immobilized lipases

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

Solvent-free enzymatic production of high quality cetyl esters.

A solvent-free biocatalytic process for the synthesis of high quality cetyl laurate, myristate, palmitate and stearate has been optimized. This enzymatic procedure follows the fundamental principles of the Green Chemistry and lead to sustainable products, which can be labeled as natural and conform to the principal requirements for its use in high value-added goods. The four esters selected are the main components of spermaceti, a mixture of waxes very appreciated in cosmetic and pharmacy because of its physical properties and emolliency, which was formerly extracted from the head of the sperm whales. In this paper, the influence of the amount of biocatalyst, the commercially available Novozym® 435, and the temperature were studied in an open-air batch reactor before carrying out the synthesis in a high performance vacuum reactor with dry nitrogen input in order to shift the equilibrium towards product formation. Under optimal conditions, conversion was higher than 98.5%. The characterization of the enzymatic cetyl esters puts in evidence that these are ultra-pure compounds, which have similar properties to the ones obtained through the conventional industrial processes with the extra benefit of being environmentally friendly

Biocatalytic Synthesis of Polymeric Esters Used as Emulsifiers

Polyglycerol polyricinoleate (PGPR) is a polymeric ester widely used as emulsifier in the food industry. In this work, PGPR biocatalytic synthesis was carried out in a onestep solvent-free enzymatic process using lipase CALB immobilized in Lewatit® Monoplus MP 64 by adsorption. The optimal immobilization conditions were determined: initial enzyme concentration of 13 mg of Lowry protein per mL phosphate buffer pH 7, and ricinoleic acid as a support activator. An immobilized derivative with 35.93 ± 4.90 mg of Lowry protein per g of dry support was obtained. It was used as a catalyst for PGPR production in open air and vacuum batch reactors, and the results obtained showed that only when the reaction equilibrium was shifted towards ester production by means of water removal, the PGPR produced fulfilled the European legislation (acid value ≤ 6 mg of KOH per g of product)

Optimization of a sustainable biocatalytic process for the synthesis of ethylhexyl fatty acids esters

Biocatalytic synthesis of ethylhexyl palmitate and ethylhexyl stearate as natural alternatives of cyclomethicone has been studied. In this work the esters have been obtained with two commercial enzymes: Novozym®435 and Novozym®40086 in a “solvent free” system. Operational conditions have been optimized using experimental design and response surface methodology. In the optimum reaction conditions conversion values were higher than 85% in one hour in all the cases. Operation in vacuum reactors with constant N2 bubbling improved the obtained results since it favours water removal and, in consequence, the shifting reaction equilibrium in the way of the synthesis. Besides, Candida antarctica lipase Novozym®435 was the most effective, reaching a conversion value of 98% in 45 min. However, cost study revealed that the process is cheaper when using Novozym®40086 in open-air reactors