Rhizopus delemar, lipase from

TIL Thermomyces lanuginosus lipase, RdL Rhizopus delemar lipase, RnL Rhizopus niveus lipase, MmE Mucor miehei esterase, PsL Pseudomonas sp. lipase, MmL Mucor miehei lipase, RoL Rhizopus orvzae lipase, CaLA Candida antarctica lipase A, CaLB Candida antarctica lipase B, PLE Pig liver esterase, EP Enteropeptidase, PKA Porcine kidney acylase, CE Cholesterol esterase Figure 8.1 (S)-Selective enzyme hits from hydrolase screening. ... 

If regio- or stereospecific lipases are used to interesterify oil blends, the products formed are different from those obtained by chemical interesterification, and may exhibit better functional properties. For example, interesterification of blends of canola and palm oils, using the in-1,3-specific Rhizopus delemar lipase as a biocatalyst, gave oils with improved fluidity compared with the original blends or chemically interesterified products. 

Shimada, Y. Sugihara, A. Nakano, H. Kura-moto, T. Nagao, T. Gemba, M. Tominaga, Y. Purification of docosahexaenoic acid by selective esterification of fatty acids from tuna oil with Rhizopus delemar lipase. J. Am. Oil Chem. Soc. 1997, 74 (2), 97-101. 

The polyesters in the form of films of 5x5 cm in size and approximately 2 mm thickness, prepared in a hydraulic press, were placed in petries containing phosphate buffer solution (pH 7.2) with 1 mg/mL Rhizopus delemar lipase. Usually enzymatic hydrolysis studies are performed at 37°C. However this temperature is very close to the melting point of PPSu. So, in this case the tests were performed at 30 1°C. The degree of biodegradation was estimated from the mass loss and molecular weight reduction as measured by GPC. 

Stmctured triacylglycerols (see Chapter 6) of the type CGC (where C represents caprylic acid, and G represents GLA) have been prepared in a two-step process. In the first stage the triacylglycerol GGG is prepared from glycerol, GLA, and Candida antarctica lipase. This is then subjected to acidolysis with caprylic acid or interesterification with ethyl caprylate in the presence of Rhizopus delemar lipase. A typical reaction product contains 53% caprylic acid and 47% GLA with CCG (58%) and CGG (29%) as the major triacylglycerols (Kawashima etal., 2001). This particular work was carried out only on a laboratory scale but there are many reports of this type of enzymatic process being carried out on a kilogram scale. At present such compounds are probably too expensive to be incorporated into functional foods and are more likely to be used in pharmaceutical preparations. 

It is easy to understand that poly(ester-urethane) is susceptible to hydrolysis by an enzyme, such as lipase and esterase. The poly(ester-urethane) was hydrolyzed by Rhizopus delemar lipase at the polyester moiety of poly(ester-urethane) (Tokiwa et al, 1988). Santerre et al (1994) and Wang et al (1997) reported that cholesterol esterase degraded poly(ester-urethane), synthesized from TDI, polycaprolactonediol and ethylene diamine, and released the hard-segment components. 

Continuous stirred-tank reactor Hydrolysis of milk fat Lipase from Rhizopus delemar 127... 

Effect of Molecular Weight of Polyester on the Hydrolysis by Rhizopus lipase. Using three kinds of polyesters, PCL-diol (I), polyhexameth-ylene adipate (II), and a copolyester (ill) made from 1,6-hexamethyl-enediol and a 70 30 molar ratio mixture of e- caprolactone and adipic acid, the effects of the of polyester on the hydrolysis by lipase were examined (Figure k) Mn did not affect the rates of hydrolysis by R. arrhizus and delemar lipases when Vln was more than about UOOO. This would indicate these lipases randomly splits ester bonds in pol-mer chains. In contrast, when TEi was less than about i4000 2 the rates of the enzymatic hydrolysis were faster with the smaller Mn of polyesters. This corresponded to the fact that Tm was lower with the smaller Mn of polyesters. 

Nakamura et al. (1986) Batch Esterification of triolein using stearic acid Lipase from Rhizopus delemar... 

Lipases that are in-1,3 specific include those from Mucor miehei, Mucor java-nicus, Aspergillus niger. Pseudomonas fluorescens, Rhizopus delemar, Rhizopus arrhizus, and pancreatic lipase (11, 25-27). These enzymes cleave the fatty acids only from the sn-l and sn-3 positions of the glycerol backbone of TAGs. Thus, with these lipases, TAGs are hydrolyzed to afford FFA, 1,2 (2,3)-DAGs and 2-MAGs. 

Hydrolysis of 2-naphthyl acetate Oi o Lipase from Rhizopus delemar n-Heptane Assuming film thickness 6 = 10 cm, enhancement is 10 times that in aqueous phase alone Miyake et al. (1991)... 

Converting olive oil to an interesterified fat (1- and 3-positionaI specific interesterification) Immobilized lipase from Rhizopus delemar Water saturated n-hexane No comparison of yields in aqueous and biphasic system available Yokozeki et al. (1982)... 

Walter, T., Augusta, J., Muller, R.-J., Widdecke, H., and Klein, J., 1995, Enzymatic degradation of a model polyester by lipase from Rhizopus delemar. Etcym. Microb. Technol 17 218-224. 

Enzymic interesterification is a recent development of considerable promise. Its advantage over the more conventional procedures lies in the additional control of product composition. The lipase, coated on to a support material (kieselguhr, hydroxylapatite, alumina) in the presence of a little water, supports interesterification at about 40 °C and usually requires 16-70 h for complete reaction but can be shorter depending on catalyst activity. The process may be operated in a batch or continuous manner. The substrate is a natural oil or fat to which may be added a second oil or fat and/or a particular fatty acid or fatty acid mixture. Three types of enzyme are available. One type (from Candida cylindricae, Coryne-bacterium acnes or Staphylococcus aureus) is nonspecific and leads to complete randomization of all acids at all positions. The product is the same as that obtained from the ordinary catalytic process. A second type of lipase (from Aspergillus niger, Mucor favanicus, Rhizopus arrhizus, / . delemar... 

The amino acid sequences of lipases from Rhizopus delemar, R. javanicus and R. niveus are identical. The sequence of the lipase from R. oryzae differs by only two conservative substitutions. The amino acid sequence and biochemical properties of the lipases fi om Pseudomonas glumae and Chromobacterium viscosum are identical see Taipa MA, Liebeton K, Costa JV, Cabral IMS, Jaeger KE (1995) Biochtm. Biophys. Acta 1256 395 Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schomburg D (1996) J. Mol. Biol. 259 704. 

Using a modified system as described by Ergan et al. (1990), an 87% conversion of medium chain fatty acids into medium chain triacylglycerols (MCTs) has been observed. However, Kim and Rhee (1991) obtained marginal amounts of tricaprin in their experiments with lipozyme and various methods of removing water from the reaction. The current interest in the use of MCTs in various food applications as fatless fats could trigger more activity in their enzymatic synthesis. Attention might be focused on short-chain specific enzymes such as lipases from Rhizopus delemar (Tahoun and Ali, 1986). 

Valis, T.P, Xenakis, A., Kolisis, F.N. 1992. Comparative studies of lipase from Rhizopus delemar in various microemulsion systems. Biocatalysis 6, 267-279. 

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