Control of lipase-mediated glycerolysis reactions with butter oil in dual liquid phase media devoid of organic solvent

Yang, Baokang; Harper, W. J.; Parkin, Kirk L.

doi:10.1021/jf00035a018

Cited by 14 publications

(11 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In reaction mixtures in which organic solvent is omitted, the same parameters influence reaction efficiency, but in a slightly different manner, as reported in the following paper (Yang et al, 1993b Although butteroil was used as the principal lipid substrate for these studies, our findings are likely to be applicable to the reactivity of other TAG-rich oils used under similar conditions.…”

Section: Discussionmentioning

confidence: 71%

Control of lipase-mediated glycerolysis reactions with butter oil in single liquid phase media with 2-methyl-2-propanol

Yang¹,

Harper²,

Parkin³

1993

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Factors affecting the progress of glycerolysis reactions with butteroil mediated by two lipase preparations (from Pseudomonas sp.) in single liquid phase mixtures containing 2-methyl-2-propanol were evaluated. Within the range of parameters evaluated, the conditions best supporting the formation of monoacylglycerols (MAG) were 25-40 % butteroil substrate, 10-20 mg of enzyme/mL of substrate mixture, 35 OC, and 100-150 mg of glycerol/mL of substrate mixture (equivalent to a molar ratio of fatty acyl groups to glycerol of 0.61-0.76). Under these conditions, the percent yield of MAG formation from butteroil was 5040% (mass fraction) relative to the other acylglycerolspecies and fatty acids accumulated. These conditions were somewhat dependent on the source of enzyme and probably related to the water content of the enzyme reagents. At temperatures greater than 35 "C, and a t the greatest levels of glycerol (150mg/mL) used, asevere restriction of activity was noted, particularly for the lipase preparation with the lesser water content. However, activity and percent yields of MAG could be restored to near-optimal levels by the simple addition of water of up to 1% of the reaction volume. The ability of the chosen lipases to mediate glycerolysis reactions with butteroil, and other oils, appears to be principally controlled by water availability in the reaction mixture.Abstract published in Advance ACS Abstracts, October 15, 1993.

show abstract

Section: Discussionmentioning

confidence: 71%

Control of lipase-mediated glycerolysis reactions with butter oil in single liquid phase media with 2-methyl-2-propanol

Yang¹,

Harper²,

Parkin³

1993

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…The baseline conditions were the same as what was outlined earlier for the enzyme screening procedures. It has been shown that little interaction exists between these critical parameters during the course of glycerolysis process (16). The reaction procedures were carried out in the same manner as in lipase screening.…”

Section: Methodsmentioning

confidence: 99%

Enzymatic glycerolysis of soybean oil

Noureddini

Harmeier

1998

J Americ Oil Chem Soc

View full text Add to dashboard Cite

Enzymatic glycerolysis of soybean oil was studied. Of the nine lipases that were tested in the initial screening, Pseudomonas sp. resulted in the highest yield of monoglycerides. Lipase from Pseudomonas sp. was further studied for the influence of temperature, thermal stability, enzyme/oil ratio, and glycerol/oil ratio. A full factorial optimization approach was performed. The following conditions were tested over the specified ranges: temperature (30–70°C), thermal stability (30–70°C), enzyme/oil ratio (0.05–0.2 g enzyme/10 g oil), glycerol/oil ratio (1:1–3:1 glycerol/oil molar ratio) and 1 h reaction time. The stability of the enzyme at the reaction temperature was also incorporated as a separate variable. At temperatures above 40°C enzyme denaturation offset the higher activity. The optimal conditions were selected to be the basis for a continuous process: 40°C, a glycerol/oil molar ratio of 2:1, and an enzyme/oil ratio of 0.1 g enzyme/10 g oil. A definition for glycerolysis activity was adopted. The glycerolysis activity (1 GU) was defined as the amount of enzyme necessary to consume 1 µmol of substrate (glycerol and oil) per minute. This research is intended to explore the reaction parameters that are important in a continuous enzymatic glycerolysis process.

show abstract

“…Chemical glycerolysis of fats and oils is used for the commercial production of monoglycerides, which are applied as emulsifiers in a wide range of fl)ods and cosmetic and pharmaceutical [ 190,191 ] Pseudomonas Monoacylglycerols (surfactants) [192][193][194][195][196][197] Chrornoba ct erium t,iscosum [ 198,199] Pseudornonas ,[luorescens [ 198] Chromobacterium riscosum [200,201] Macrocyclic lactones [213,214] products. It is not likely that this process will be replaced by an enzymatic process in the near future, although labscale enzymatic glycerolysis of various fats and oils has been described [192][193][194][195][196][197].…”

Section: Glycerolysismentioning

confidence: 99%

“…The reaction temperature should be below a certain critical value [192,195,196], which was also dependent on the type of fat or oil [192]. In addition, the water content of the reaction mixture was shown to be a critical factor [195,196]. Several fungal lipases were shown to be inactive [193].…”

Section: Glycerolysismentioning

confidence: 99%

Bacterial lipases

Jaeger

1994

FEMS Microbiology Reviews

212

233

View full text Add to dashboard Cite

Many different bacterial species produce lipases which hydrolyze esters of glycerol with preferably long-chain fatty acids. They act at the interface generated by a hydrophobic lipid substrate in a hydrophilic aqueous medium. A characteristic property of lipases is called interfacial activation, meaning a sharp increase in lipase activity observed when the substrate starts to form an emulsion, thereby presenting to the enzyme an interfacial area. As a consequence, the kinetics of a lipase reaction do not follow the classical Michaelis-Menten model. With only a few exceptions, bacterial lipases are able to completely hydrolyze a triacylglycerol substrate although a certain preference for primary ester bonds has been observed. Numerous lipase assay methods are available using coloured or fluorescent substrates which allow spectroscopic and fluorimetric detection of lipase activity. Another important assay is based on titration of fatty acids released from the substrate. Newly developed methods allow to exactly determine lipase activity via controlled surface pressure or by means of a computer-controlled oil drop tensiometer. The synthesis and secretion of lipases by bacteria is influenced by a variety of environmental factors like ions, carbon sources, or presence of non-metabolizable polysaccharides. The secretion pathway is known for Pseudomonas lipases with P. aeruginosa lipase using a two-step mechanism and P. fluorescens lipase using a one-step mechanism. Additionally, some Pseudomonas lipases need specific chaperone-like proteins assisting their correct folding in the periplasm. These lipase-specific foldases (Lif-proteins) which show a high degree of amino acid sequence homology among different Pseudomonas species are coded for by genes located immediately downstream the lipase structural genes. A comparison of different bacterial lipases on the basis of primary structure revealed only very limited sequence homology. However, determination of the three-dimensional structure of the P. glumae lipase indicated that at least some of the bacterial lipases will presumably reveal a conserved folding pattern called the alpha/beta-hydrolase fold, which has been described for other microbial and human lipases. The catalytic site of lipases is buried inside the protein and contains a serine-protease-like catalytic triad consisting of the amino acids serine, histidine, and aspartate (or glutamate). The Ser-residue is located in a strictly conserved beta-epsilon Ser-alpha motif. The active site is covered by a lid-like alpha-helical structure which moves away upon contact of the lipase with its substrate, thereby exposing hydrophobic residues at the protein's surface mediating the contact between protein and substrate.(ABSTRACT TRUNCATED AT 400 WORDS)

show abstract

Control of lipase-mediated glycerolysis reactions with butter oil in dual liquid phase media devoid of organic solvent

Cited by 14 publications

References 13 publications

Control of lipase-mediated glycerolysis reactions with butter oil in single liquid phase media with 2-methyl-2-propanol

Control of lipase-mediated glycerolysis reactions with butter oil in single liquid phase media with 2-methyl-2-propanol

Enzymatic glycerolysis of soybean oil

Bacterial lipases

Contact Info

Product

Resources

About