Continuous reactor for enzymic glycerolysis of butteroil in the absence of solvent

Garcı́a, Hugo S.; Yang, Baokang; Parkin, Kirk L.

doi:10.1016/0963-9969(95)00051-8

Cited by 24 publications

(17 citation statements)

References 23 publications

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“…4) suggest that the interaction between the lipase and the polypropylene support was strong, since no change in residual activity was observed in immobilized lipases after washing them with phosphate buffer during 12 h at room temperature and 250 rpm. Previous works have reported that strong hydrophobic forces keep lipase bound to hydrophobic supports [8,9]. The addition of NaCl in washing buffer did not alter the activity of lipase immobilized without Triton X-100, but the lipase immobilized in the presence of the detergent lost 27.5% of its activity, probably because lipase molecule is in its monomeric form and more evenly distributed on the support surface making it more susceptible to desorption when ionic strength was changed [23].…”

Section: Desorption Of the Immobilized Lipasementioning

confidence: 81%

“…Under these conditions, we found up to 40% increase in lipase specific activity after immobilization. The increase in specific activity of lipases immobilized on hydrophobic supports has been reported [8,9,24]; the authors propose that this activity increase is caused by a strong interaction of hydrophobic areas of lipases near/on the lid with the support surface, which leads to conformational changes that result in a highly active open form.…”

Section: Lipase Immobilizationmentioning

confidence: 95%

“…Lipases are commonly activated by interactions with hydrophobic interfaces, due to conformational changes in their secondary structures. Thus adsorption to hydrophobic supports such as polypropylene, have been the most widely used methods for lipase immobilization [7][8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase

Sánchez-Otero

Valerio‐Alfaro

García-Galindo

et al. 2008

J Ind Microbiol Biotechnol

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A partially purified lipase produced by the thermophile Geobacillus thermoleovorans CCR11 was immobilized by adsorption on porous polypropylene (Accurel EP-100) in the presence and absence of 0.1% Triton X-100. Lipase production was induced in a 2.5% high oleic safflower oil medium and the enzyme was partially purified by diafiltration (co. 500,000 Da). Immobilization conditions were established at 25 degrees C, pH 6, and a protein concentration of 0.9 mg/mL in the presence and absence of 0.1% Triton X-100. Immobilization increased enzyme thermostability but there was no change in neither the optimum pH nor in pH resistance irrelevant to the presence of the detergent during immobilization. Immobilization with or without Triton X-100 allowed the reuse of the lipase preparation for 11 and 8 cycles, respectively. There was a significant difference between residual activity of immobilized and soluble enzyme after 36 days of storage at 4 degrees C (P < 0.05). With respect to chain length specificity, the immobilized lipase showed less activity over short chain esters than the soluble lipase. The immobilized lipase showed good resistance to desorption with phosphate buffer and NaCl; minor loses with detergents were observed (less than 50% with Triton X-100 and Tween-80), but activity was completely lost with SDS. Immobilization of G. thermoleovorans CCR11 lipase in porous polypropylene is a simple and easy method to obtain a biocatalyst with increased stability, improved performance, with the possibility for re-use, and therefore an interesting potential use in commercial conditions.

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Section: Desorption Of the Immobilized Lipasementioning

confidence: 81%

Section: Lipase Immobilizationmentioning

confidence: 95%

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Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase

Sánchez-Otero

Valerio‐Alfaro

García-Galindo

et al. 2008

J Ind Microbiol Biotechnol

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“…Therefore, EstTB11 is an induction-type esterase; however, its productivity was sharply inhibited on triolein as an inducer. At present, reports are available regarding the hydrolysis of olive oil [26], butter oil [27], beef tallow [28] and other animal fats [29] using lipase, but data on the use of single cream inducing Pseudomonas for the production of esterase have not been reported. In this study, the experiment proved successfully improving EstTB11 activity by induction of Pseudomonas sp.TB11 with single cream.…”

Section: Discussionmentioning

confidence: 95%

A novel extracellular cold-active esterase of Pseudomonas sp. TB11 from glacier No.1: Differential induction, purification and characterisation

Dong

Zhao

Gasmalla

et al. 2015

Journal of Molecular Catalysis B: Enzymatic

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“…Mild reaction conditions afforded by enzymatic processes also help reduce the overall energy consumption greatly improving industry economics [8,9]. Wide amount of literature is available on enzymatic production of monoacylglycerols of different fatty acids using various types of lipases under different reaction conditions by mainly two routes namely esterification between glycerol and fatty acid and glycerolysis of vegetable oil [4,[10][11][12]. Glycerolysis of oils is not favored when the target product is monoglyceride because it leads to a mixture of mono, di and triglycerides and repeated molecular distillation steps are needed to obtain pure product.…”

Section: Introductionmentioning

confidence: 99%

Production of Glyceryl Monostearate by Immobilized Candida Antarctica B Lipase in Organic Media

Odaneth¹

2017

JABB

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Chemical methods of synthesizing monoglycerides (MGs) produce mixture of acylglycerols making the synthesis of MGs of a single fatty acid type not possible through this route. Lipases due to their selectivity and specificity offer a useful way of synthesizing highly purified single fatty acid containing monoglycerides. Glyceryl monostearate (GMS), a nonionic amphiphilic monoglyceride of glycerol and stearic acid is widely used as emulsifier in food, cosmetic, pharmaceutical and textile industry. In the present work, lipase mediated synthesis of GMS was explored using Novozym 435 and indigenously immobilized Candida antarctica B lipase. Direct esterification of glycerol and stearic acid was used as strategy and various parameters that influence synthesis of glyceryl monostearate such as molar ratio of substrates, enzyme load, reaction time and solvent polarity were systematically studied using Novozym 435 lipase. Esterification efficiency of indigenously immobilized Candida antarctica B lipase and Novozym 435 was compared for synthesis of GMS and indigenously immobilized Candida antarctica B lipase gave conversion competitive to Novozym 435. Indigenously immobilized Candida antarctica B lipase in the presence of homogenous substrate solution using tert-butyl alcohol as the reaction medium, resulted in exclusive production of monoglyceride without formation of diglyceride. Continuous production of GMS was also carried out in packed bed reactor and 94% conversion of stearic acid was achieved.

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Continuous reactor for enzymic glycerolysis of butteroil in the absence of solvent

Cited by 24 publications

References 23 publications

Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase

Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase

A novel extracellular cold-active esterase of Pseudomonas sp. TB11 from glacier No.1: Differential induction, purification and characterisation

Production of Glyceryl Monostearate by Immobilized Candida Antarctica B Lipase in Organic Media

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