Production and optimization of isopropyl palmitate via biocatalytic route using home‐made enzymatic catalysts

Barsé, Laísa Quadros; Graebin, Natália G.; Cipolatti, Eliane Pereira; Robert, Julia de Macedo; Pinto, Maria do Carmo F. R.; Pinto, Jose Ccs; Freire, Denise M. G.; Rodrigues, Rafael C.

doi:10.1002/jctb.5782

Cited by 16 publications

(2 citation statements)

References 55 publications

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“…They belong to the class of hydrolases (EC 3.1.1.1) and their natural function is the hydrolysis of triglycerides to fatty acids and glycerol. Nevertheless, under non-aqueous conditions, lipases are able to catalyze a broad range of reactions such as esterification, transesterification, and interesterification or acidolysis [165][166][167][168][169][170][171][172][173][174][175][176][177]. Moreover, besides this broad range of reactions, lipases are able to recognize a vast diversity of substrates, being able to catalyze even promiscuous reactions [178,179].…”

Section: Lipases As Industrial Biocatalystsmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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Section: Lipases As Industrial Biocatalystsmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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“…Polystyrene as a macroporous resin is more suitable for enzyme supports because of its high‐specific surface area and hydrophobicity. These characteristics facilitate immobilization, increase enzyme‐loading capacity, and enhance thermal stability …”

Section: Introductionmentioning

confidence: 99%

Prediction and comparison of textural properties of magnetic copolymer supports for enzyme immobilization

Rosa

Silva

Aguiar

et al. 2020

J of Applied Polymer Sci

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Magnetic polymers supports have proven to be valuable materials for enzyme immobilization, as they allow recovering the catalyst by magnetic separation, precluding the need for costly and time‐consuming separation steps. In this study, magnetic copolymer supports were synthesized using styrene (STY) and different crosslinking agents (divinylbenzene, ethylene glycol dimethacrylate, or triethylene glycol dimethacrylate) and initiators (azobisisobutyronitrile or benzoyl peroxide) and used to immobilize Candida antarctica lipase B (CALB). The aim was to obtain biocatalysts with high enzymatic activity and satisfactory morphological properties for use in biotransformation reactions. Two morphological properties known to influence the immobilization yield were taken into consideration, specific surface area, and swelling index. Experimental data were compared to the predictions of a model based on molar balance, method of moments, numerical fractionation, and elementary gel structures. The high correlation (R2 = 0.9974) between experimental and predicted values demonstrated the suitability of the model for estimating the textural properties of enzyme supports. CALB was successfully immobilized, showing high hydrolytic activity (500–700 U g−1) and good thermal stability at 50°C. CALB/STY‐EGDMA‐M was 14 times more stable than free CALB. The results confirm the efficiency of the immobilization method and the suitability of the copolymers for enzyme immobilization.

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Polymerization strategies to produce new polymer biocatalysts for the biodiesel industry

Pinto

Sousa

Dutra

et al. 2021

J of Applied Polymer Sci

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One of the major challenges regarding the enzymatic production of biodiesel is the development of more robust, active, and stable immobilized biocatalysts. Thus, the present work aims to develop new enzymatic biocatalysts for use in esterification and transesterification reactions. New polymer supports based on poly(styrene-co-divinylbenzene) and poly(methyl methacrylate-co-divinylbenzene) platforms were synthesized, incorporating distinct functional compounds into the polymer chains (1-octene, cardanol, and vinyl benzoate). Two distinct polymerization strategies were adopted for support syntheses: (i) Combined suspension and emulsion polymerization process (core-shell particles); and (ii) Two-step polymerization reaction comprising a suspension polymerization in presence of porogenic agents, followed by vacuum application (porous and nonporous particles). The obtained particles were employed for immobilization of lipase B from Candida antarctica. The addition of functional compounds resulted in particles with distinct textural properties. Moreover, particles with 91 m 2 .g À1 (P(MMA-co-DVB)/ P(MMA-co-DVB)) were produced through combined suspension and emulsion polymerization, whilst particles with 154 m 2 .g À1 (P[MMA-co-DVB-co-VB]) were produced through suspension polymerization performed in presence of n-heptane. Moreover, highly active biocatalysts were produced, leading to esterification conversions above 80%. Thus, based on the performance in esterification and transesterification reactions, the new functional matrices resulted in highly active biocatalysts with good potential for use in biodiesel industry.

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Production and optimization of isopropyl palmitate via biocatalytic route using home‐made enzymatic catalysts

Cited by 16 publications

References 55 publications

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Prediction and comparison of textural properties of magnetic copolymer supports for enzyme immobilization

Polymerization strategies to produce new polymer biocatalysts for the biodiesel industry

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