Screening of commercial lipases for production of mono- and diacylglycerols from butteroil by enzymic glycerolysis

Yang, Baokang; Harper, W. J.; Parkin, Kirk L.; Chen, Jyh‐Ping

doi:10.1016/0958-6946(94)90045-0

Cited by 33 publications

(34 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The enzymes used in this study are reported to be regioselective (and not regiospecific) for the sn-1,3 positions along the glycerol backbone in terms of hydrolytic activity (Berger and Schneider, 1991) but nonspecific in terms of esterification activity between FA and glycerol . The relationship, if any, between hydrolytic and glycerolysis or other lipase activities is not clear or predictable (Yang et al, 1993a; V o r d e d b e c k e et al, 1992). These enzymes were chosen for study because, of those screened by us (Yang et al, 1993a), they best supported glycerolysis and did so equally well in the presence or absence of solvent.…”

Section: Resultsmentioning

confidence: 99%

“…Our initial efforts to prepare mixtures of MAG and DAG from butteroil focused on the screening of several lipases for their ability to promote glycerolysis reactions with butteroil (Yang et al, 1993a). Reactivity was dependent on the source of lipase and whether reaction mixtures contained an organic solvent as the principal component of the continuous phase.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

“…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%

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

“…To prevent the generation of dark-colored by-products with undesirable fiavors, Iow-temperature MAG synthesis using lipase has been attempted by many researchers. There are two main enzymatic pathways to yield MAG; ester synthesis from free fatty acid and glycerol (Tsujisaka et al, 1977;Hoq et al, 1984;Schuch & Mukherjee, 1989;Akoh et al, 1992;van der Padt et al, 1992;Berger & Schneider, 1992b;Li & Ward, 1993), and glycerolysis ofedible fats and oils (Yamane et al, 1986~, b;Holmberg et al, 1989;Yang et al, 1994a, b).…”

Section: A Iarge Quantity Of Monoacylglycerols (Mag) Is Used Asmentioning

confidence: 99%

Synthesis of Either Mono-or Diacylglycerol from High-Oleic Sunflower Oil by Lipase-Catalyzed Glycerolysis.

Ota

Takasugi

Suzuki

1997

FSTI

View full text Add to dashboard Cite

The difference in reaction conditions between the syntheses of mono-and diacylglycerols (MAG and DAG) was elucidated in terms of the enzymatic glycerolysis of high-oleic sunflower oil containing 89% oleic acid. The most efficient lipases were Pseudomonas lipoprotein lipase and the lipase from Pseudomonas cepacia for the MAG and DAG syntheses, respectively. In each case, the glycerol amount to be added to maximize the yield was 1.5-fold larger than the stoichiometric amount that is necessary to complete the glycerolysis reaction. The addition of a small amount of acetone to the reaction mixture was only slightly effective on the yield of MAG. The control of the reaction temperature was very important, and the critical temperature, below which the yield of MAG or DAG is significantly increased, was found to be lower for DAG synthesis than for MAG synthesis. The reaction time that was required to obtain a maximum yield was about 80 h for MAG synthesis, while it was 6-fold longer for DAG synthesis. The content of MAG and monooleoylglycerol approached 90 and 80% in the lipid reaction products, respectively. On the other hand, the content of DAG was 82%, of which the fatty acid composition was similar to that of the original oil.Keywords: acetone, monooleoylglycerol, glycerolysis, high-oleic sunfiower oil, Iipase, monoacylglycerol, diacylglycerol A Iarge quantity of monoacylglycerols (MAG) is used as emulsifying agents in the manufacture of foods and cosmetics.

show abstract

Screening of commercial lipases for production of mono- and diacylglycerols from butteroil by enzymic glycerolysis

Cited by 33 publications

References 22 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

Bacterial lipases

Synthesis of Either Mono-or Diacylglycerol from High-Oleic Sunflower Oil by Lipase-Catalyzed Glycerolysis.

Contact Info

Product

Resources

About