Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase

Käämbre, Tuuli; Tõugu, Vello; Käämbre, Peeter; Vija, Heiki; Sikk, Peeter

doi:10.1016/s0167-4838(99)00047-3

Cited by 7 publications

(9 citation statements)

References 39 publications

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“…The desirability function was performed in Design-Expert 7.1.3, and each response was assigned an important value (1)(2)(3)(4)(5). The objective function is given as follows:…”

Section: Experiments Designmentioning

confidence: 99%

“…Free fatty acids (FFA), the raw material of oleochemistry, are produced predominantly from the hydrolyzed natural triacylglycerols of vegetable oils or animal fats. For the enzymatic reaction, substrate concentration, temperature, enzyme loading, reaction time, shaking rate and pH value could affect the enzymatic hydrolysis efficiency significantly [2][3][4][5][6]. Furthermore, the possible interaction of multiple variables may also influence the output [7].…”

Section: Introductionmentioning

confidence: 99%

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Optimization of Enzymatic Hydrolysis of Chicken Fat in Emulsion by Response Surface Methodology

Teng¹,

Le²,

Yuan³

et al. 2009

J Americ Oil Chem Soc

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Chicken fat in an emulsion prepared with mechanical shearing and high pressure homogenization (HPH) was hydrolyzed using Candida cylindracea lipase. A homogenization pressure of 50 MPa, which can generate smaller droplets and higher hydrolysis efficiency than mechanical shearing, was fixed to prepare the emulsion for hydrolysis optimization. Response surface methodology (RSM) was applied to study the effect of temperature, enzyme loading, shaking rate and reaction time on the hydrolysis process. The results showed that all three-second-order polynomial models adequately fitted the experimental data. Additionally, hydrolysis parameters for the optimal yields of free oleic and linoleic acids were also obtained using the desirability function: a temperature of 38°C, an enzyme loading of 0.48% (g/g fat basis), a shaking rate of 100 rpm and a reaction time of 80 min. Under the optimal conditions, the yields of free oleic and linoleic acids were predicted as being 0.470 and 0.118 g/g fat with recoveries of 94.6 and 93.7%, respectively. During the hydrolysis process, the particle size increased with concomitant boosting of the degree of hydrolysis and the stability of the emulsion system was gradually undermined by this reaction process.

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“…The desirability function was performed in Design-Expert 7.1.3, and each response was assigned an important value (1)(2)(3)(4)(5). The objective function is given as follows:…”

Section: Experiments Designmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Optimization of Enzymatic Hydrolysis of Chicken Fat in Emulsion by Response Surface Methodology

Teng¹,

Le²,

Yuan³

et al. 2009

J Americ Oil Chem Soc

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“…[25] In this sense, it has been pointed out that the high mutual solubility of triacetin and water probably results in the formation of a diffuse and poorly hydrophobic interface. [26] This hypothesis has been useful to explain the lack of interfacial activation of the R. miehei lipase with triacetin, enzyme that however does show activation with other substrates. [27] These results emphasised the importance of the enzyme binding step in the overall lipolysis rate and suggested that the low activity of Lip1 on triacetin in the absence of hexane, compared to that Lip3 (Fig.…”

Section: Activation Under Kinetic Conditionsmentioning

confidence: 99%

Regulation of the interfacial activation within the Candida rugosa lipase family

Pernas¹,

Pastrana²,

Fuciños³

et al. 2009

J of Physical Organic Chem

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The fungus Candida rugosa produces several lipase isoenzymes and the 3D structure of three was solved (Lip1, Lip2 and Lip3). In an aqueous solution, the hydrophobic catalytic cavity of these lipases is buried under a flap that blocks the entrance of the substrate. In the hydrolysis of triacetin, the limiting step of the catalytic process was the activation of the enzyme and only the existence of the highly hydrophobic interface provided by hexane was able to shift the equilibrium towards the open conformation. In the case of Lip1, the hexane interface was crucial and once the open conformation was stabilised, Lip1 was as efficient as Lip3 for the hydrolysis of triacetin. Lip2 isoenzyme behaves more similarly to mLip3 reinforcing the higher structural and functional similarity between these isoenzymes. Inhibition experiments carried out under non-kinetic conditions allowed to correlate the higher flexibility of the closed flap and the higher hydrophobicity of the catalytic pocket of mLip3 with the greater facility of this isoenzyme to become activated by interfaces of different chemical nature. Both factors might allow a more intense penetration of mLip3 into the interfaces. In these systems, we observed a unique behaviour of Lip2, enzyme that although in a monomeric state and provide with an analogous flap structure to that of Lip1 or Lip3 underwent a very fast activation even in the absence of supramicellar concentrations of surfactants. We determined that the inhibitor itself forms micelles and hypothesised that they might provide an adequate interface for Lip2 activation.

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“…3,4,8,9 However, such a reaction system does not reflect the dietary fat digestion contained in food. 3,4,8,9 However, such a reaction system does not reflect the dietary fat digestion contained in food.…”

Section: Effect Of Colipase On Pl Hydrolysismentioning

confidence: 99%

“…1,2 Most studies of this lipase hydrolysis of glycerides have been carried out titrimetrically on a pH-stat. 5,6,9 Because the increment of the length of the side-chain in a glyceride increases its insolubility in an aqueous solution, difficulty was found in measurements of lipase hydrolysis using such insoluble substrates. As a result, this method necessitates the use of a large amount of expensive enzyme.…”

Section: Introductionmentioning

confidence: 99%

Fluorimetric analysis of lipase hydrolysis of intermediate- and long-chain glycerides

Tsuzuki

Nagao

et al. 2002

Analyst

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For the purpose of deducing the digestive behavior of dietary fat in the digestive organs, a fluorimetric method for the measurement of hydrolysis by porcine pancreatic lipase was performed using intermediate- and long- acyl chain glycerides as substrates. Insoluble glycerides constituted by C10-C16 acyl chains were mechanically dispersed in 100% buffer and hydrolyzed by porcine pancreatic lipase. After the reaction, fatty acid released by the enzyme was extracted and its carboxyl group was fluorescently labeled with 9-bromomethylacridine. The 9-acridinylmethyl derivative of the fatty acid was separated and determined by HPLC. The sensitivity of this method was about 1000 times higher than that of the titrimetric method. Only 0.5 ng of porcine pancreatic lipase was sufficient for one routine assay. This assay method was successfully applied to investigate the enzymatic properties of porcine pancreatic lipase with respect to dietary lipids. The effects of some physiological factors concerned with lipid digestion, such as bile salt and colipase, on the lipase hydrolysis were also examined. The method established in the present study could contribute to a highly sensitive assay of some hydrolases containing lipase with regard to insoluble substrates.

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Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase

Cited by 7 publications

References 39 publications

Optimization of Enzymatic Hydrolysis of Chicken Fat in Emulsion by Response Surface Methodology

Optimization of Enzymatic Hydrolysis of Chicken Fat in Emulsion by Response Surface Methodology

Regulation of the interfacial activation within the Candida rugosa lipase family

Fluorimetric analysis of lipase hydrolysis of intermediate- and long-chain glycerides

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