Kinetics of the enzymatic hydrolysis of triglycerides in o/w emulsions

Jurado, E.; Camacho, F.; Luzón, G.; Fernández-Serrano, Mercedes; García-Román, Miguel

doi:10.1016/j.bej.2008.02.002

Cited by 41 publications

(37 citation statements)

References 29 publications

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“…The error bars indicate the standard deviation between the eight substrate control trials. Hydrolysis of tributyrin was always faster than that of cellulose, as found in literature [24] [16]. Similar to the results from the cellulose trials, the average hydrolysis rate found for all eight tributyrin substrate control trials was faster in the beginning of the experiment, followed by a slower rate after approximately 8 h, which resulted in a k h seven times higher for the first 8 h, as shown in Fig.…”

Section: Tributyrin Hydrolysissupporting

confidence: 82%

Humic Acid-Like and Fulvic Acid-Like Inhibition on the Hydrolysis of Cellulose and Tributyrin

2014

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Enzymatic hydrolysis of complex wastes is a critical step for efficient biogas production in anaerobic digesters. Inhibition of this hydrolytic step was studied by addition of humic acid-like (HAL) and fulvic acid-like (FAL) substances, extracted from maize silage and fresh cow manure, to batch tests with cellulose and cellulases from Aspergillus niger and tributyrin and lipases from Candida rugosa. To confirm the inhibition results, microbially catalysed hydrolysis trials were performed, where Fibrobacter succinogenes was grown exclusively on cellulose. Hydrolysis products, as glucose, glycerol and butyric acid, were measured to determine the hydrolysis efficiency and its rate. Cellulose hydrolysis was inhibited by 0.5 to 5.0 g l −1 of HAL and FAL substances extracted from maize and cow manure, which are relevant concentrations for manure and maize digestion. Tributyrin hydrolysis, on the other hand, was only inhibited by 0.5 to 5.0 g l −1 of HAL substances extracted from maize and cow manure and not by FAL substances.

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Section: Tributyrin Hydrolysissupporting

confidence: 82%

Humic Acid-Like and Fulvic Acid-Like Inhibition on the Hydrolysis of Cellulose and Tributyrin

2014

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“…Many kinetic models have been proposed for the hydrolysis of triglyceride in biphasic and emulsion systems using suspended enzymes [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18]. The hydrolysis takes place at the oil-water interface, so the differences in the interfacial and bulk concentrations of the enzyme, substrates and products, and the reaction at the interface should be considered.…”

Section: Introductionmentioning

confidence: 99%

Rigorous kinetic model considering positional specificity of lipase for enzymatic stepwise hydrolysis of triolein in biphasic oil–water system

Hermansyah

Wijanarko

Kubo

et al. 2009

Bioprocess Biosyst Eng

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A rigorous kinetic model describing the stepwise triglyceride hydrolysis at the oil-water interface, based on the Ping Pong Bi Bi mechanism using suspended lipase having positional specificity, was constructed. The preference of the enzyme to cleave to the ester bonds at the edge and the center of the glycerol backbone of the substrates (tri-, di- or monoglyceride) was incorporated in the model. This model was applied to the experimental results for triolein hydrolysis using suspended Porcine pancreatic lipase (an sn-1,3 specific lipase) and Candida rugosa lipase (a non-specific lipase) in a biphasic oil-water system under various operating conditions. In order to discuss the model's advantages, other models that do not consider the positional specificity of the lipase were also applied to our experimental results. The model considering the positional specificity of the lipase gave results which fit better with the experimental data and described the effect of the initial enzyme concentration, the interfacial area, and the initial concentrations of triolein on the entire process of the stepwise triolein hydrolysis. This model also gives a good representation of the rate for cleaving the respective ester bonds of each substrate by each type of lipase.

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“…Note, it is assumed the size of the various enzyme substrate complexes don't vary significantly from the size of the free enzyme (Jurado et al 2008).…”

Section: Model Formulationmentioning

confidence: 99%

Fed-Batch Feeding Strategies for Enzymatic Biodiesel Production

Price

Nordblad

Woodley

et al. 2014

IFAC Proceedings Volumes

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Abstract:In this work a kinetic model for the enzymatic transesterification of rapeseed oil using a solubilised lipase (Callera Trans L-Thermomyces lanuginosus) was developed from first principles. The model is based on a Ping-Pong Bi-Bi mechanism, with methanol inhibition, along with consideration of the differences in the interfacial and bulk concentrations of the enzyme. The model is then used to evaluate various feeding strategies to improve the enzymatic biodiesel production. The feeding strategies investigated, gave insight into how the methanol should be fed to potentially mitigate enzyme deactivation while improving the biodiesel yield. The best experimental results gave a yield of 703.76 g FAME L -1 and a reactor productivity of 28.12 g FAME L -1 h -1 . In comparison, to reach the same yield, the optimised two step feeding strategy took 6.25 hours less, which equates to an increase the reactor productivity of 36.9 %.

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Kinetics of the enzymatic hydrolysis of triglycerides in o/w emulsions

Cited by 41 publications

References 29 publications

Humic Acid-Like and Fulvic Acid-Like Inhibition on the Hydrolysis of Cellulose and Tributyrin

Humic Acid-Like and Fulvic Acid-Like Inhibition on the Hydrolysis of Cellulose and Tributyrin

Rigorous kinetic model considering positional specificity of lipase for enzymatic stepwise hydrolysis of triolein in biphasic oil–water system

Fed-Batch Feeding Strategies for Enzymatic Biodiesel Production

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