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Rhizopus delemar lipase

Naoe et al. [239] used the sugar ester DK-F-110, a mixture of sucrose esters of fatty acids, as a nonionic surfactant along with isopropyl alcohol and hexane in a reverse micellar system to extract cytochrome C. This surfactant has a critical micellar concentration of 0.5 g/1 and HLB of 11. Aqueous phase pH was found to have a major role in the forward extraction and optimum extraction was achieved at pH 8.0. However, for optimum back extraction, addition of isopropyl alcohol at 20 vol.% was found to be very essential. Further, the esterification reaction rate of Rhizopus delemar lipase was found to be maximum in DK-F-110 systems and also higher than those obtained in AOT and lecithin-RMs at a water concentration of 0.25 mol l h... [Pg.164]

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. ... [Pg.167]

Shimada, Y., Sugihara, A., Yodono, S., Nagao, T., Maruyama, K., Nakano, H., Komemushi, S., and Tominaga, Y. 1997c. Enrichment of ethyl docosahexaenoate by selective alcoholysis with immobilized Rhizopus delemar lipase./. Ferment. Bioeng., 84,138-143. [Pg.81]

Rhizopus delemar lipase ribonucleotide reductase ring-opening metathesis Strecker three-component reaction... [Pg.629]

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. [Pg.1936]

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. [Pg.3189]

Table 11.1-11. Lipase-catalyzed enantiotopos-differentiating hydrolysis of prochiral cyclic diol dialkanoates in aqueous solution (CCL Candida cylindracea lipase, PFL Pseudomonas jiuorescens lipase, MML Mucor miehei lipase, CVL Chromobacterium viscosum lipase, PPL pig pancreas lipase, MJL Mucor javanicus lipase, RSL Rhizopus sp. lipase, PCL Pseudomonas cepacia lipase, CCL, Ceotricum candidum lipase, ANL Aspergillus niger lipase, FSPC Fusarium solani pisi cutinase, CRL Candida rugosa lipase, CAL-B Candida antarctica B lipase, LIP Pseudomonas sp. lipase-Toyobo, RDL Rhizopus delemar lipase, MSL Mucor sp. lipase, CAL Candida antarctica lipase, not specified). Table 11.1-11. Lipase-catalyzed enantiotopos-differentiating hydrolysis of prochiral cyclic diol dialkanoates in aqueous solution (CCL Candida cylindracea lipase, PFL Pseudomonas jiuorescens lipase, MML Mucor miehei lipase, CVL Chromobacterium viscosum lipase, PPL pig pancreas lipase, MJL Mucor javanicus lipase, RSL Rhizopus sp. lipase, PCL Pseudomonas cepacia lipase, CCL, Ceotricum candidum lipase, ANL Aspergillus niger lipase, FSPC Fusarium solani pisi cutinase, CRL Candida rugosa lipase, CAL-B Candida antarctica B lipase, LIP Pseudomonas sp. lipase-Toyobo, RDL Rhizopus delemar lipase, MSL Mucor sp. lipase, CAL Candida antarctica lipase, not specified).
Klein, R., G. King, R. Moreau, and M. Haas. 1997. Altered Acyl Chain Length Specificity of Rhizopus Delemar Lipase through Mutagenesis and Molecular Modeling. Lipids 32 (2) 123-130. [Pg.37]

Nagayama, K., Matsura, S., Doi, T., Imai, M. 1998. Kinetic characterization of esterification catalyzed by Rhizopus delemar lipase in lecithin-AOT microemulsion systems. J. Mol. Catal. B Enzym. 4, 25-32. [Pg.382]

Tokiwa, Y., Suzuki, T. Hydrolysis of polyesters by Rhizopus delemar lipase, Agric. Biol. Chem. 42 (1978) 5, p. 1071 - 1072... [Pg.1401]

Two-step synthesis Rhizopus delemar lipase immobilized on EP 100 MTBE/ n-hexane 91.2 71.8 Soumanou et al (1998a)... [Pg.161]

The successful transfer of these findings to the synthesis of sTAG was first demonstrated by Soumanou et al (1998a). As MTBE is not allowed for food applications, alternative solvent systems had to be identified. In addition, methods for isolating 2-MAG, as well as suitable methods for the second reaction step (esterification of the 2-MAG with free fatty acids or fatty acid esters) had to be developed. Both reactions are rather fast (approximately 4-8 h for the first step 1-3 h for the second step). The best results were obtained using Rhizopus delemar lipase as the catalyst at a =0.11 (Soumanou et al., 1999). [Pg.161]

Modified after Shimada et al. (1996). "Acidolysis between tuna oil and caprylic acid, catalysed by Rhizopus delemar lipase. ND, not detectable. [Pg.166]

Y (1996) Production of structured lipid containing docosahexaenoic and caprylic acids using immobilized Rhizopus delemar lipase. J. Ferment. Bioeng., 81, 299-303. [Pg.181]

Borage oil (22% GLA) is hydrolysed completely Pseudomonas species, 35°C, 24 h) and the borage acids are selectively esterified with lauric alcohol in the presence of Rhizopus delemar lipase at 30 C for 20 h. The latter enzyme discriminates against GLA and this concentrates in the unesterified acids fraction, which finally contains 70% GLA (74% recovery). If the esterification is repeated (using Candida rugosa lipase, 35 C, 15 h), 94% GLA is obtained with 68% recovery (Shimada et al 1997). [Pg.277]

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. [Pg.157]

Figure 8. Variation of the weight of specimens of a) PPSu, PESu and PBSu during enzymatic hydrolysis using Rhizopus delemar lipase and b) PPAd, PEAd and PBSu during enzymatic hydrolysis using 0.09 mg/mL Rhizopus delemar lipase and 0.01 mg/mL of Pseudomonas Cepacia Hpase. Figure 8. Variation of the weight of specimens of a) PPSu, PESu and PBSu during enzymatic hydrolysis using Rhizopus delemar lipase and b) PPAd, PEAd and PBSu during enzymatic hydrolysis using 0.09 mg/mL Rhizopus delemar lipase and 0.01 mg/mL of Pseudomonas Cepacia Hpase.

See other pages where Rhizopus delemar lipase is mentioned: [Pg.224]    [Pg.532]    [Pg.628]    [Pg.137]    [Pg.204]    [Pg.532]    [Pg.60]    [Pg.354]    [Pg.235]    [Pg.235]    [Pg.735]    [Pg.83]    [Pg.84]    [Pg.60]    [Pg.56]    [Pg.145]    [Pg.22]    [Pg.152]    [Pg.157]    [Pg.155]    [Pg.159]    [Pg.165]    [Pg.278]    [Pg.157]   
See also in sourсe #XX -- [ Pg.418 ]




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