Rhizopus delemar

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

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... 

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. ... 

Rhizoctoma spp. Rhizofiltration Rhizopusarrhizus Rhizopus delemar Rhizopus nigricans Rhizopus oligo sporus... 

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

Fukumoto, J., Iwai, M., Tsujisaka, Y. 1964. Studies on lipase. II. Purification and properties of a lipase secreted by Rhizopus delemar. J. Gen. Appl. Microbiol. 10, 257-265. 

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. 

Rhizopus delemar lipase ribonucleotide reductase ring-opening metathesis Strecker three-component reaction... 

The Aspergillus niger enzyme contained o-mannose, D-glucose, and D-galactose, whereas that from Rhizopus delemar contained D-mannose and 2-amino-2-deoxy-D-glucose. 

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. 

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. 

Shiraishi et al. [49,50] immobilized glucoamylase of Rhizopus delemar in monolith structures and used them for saccharification of soluble starch. The process was studied at first in a batch reactor at SOX and 4.5 bar. The simplified kinetic model was developed. A continuous process was realized in a monolith reactor consisting of 10 pieces stacked on top of each other, where the blocks were rotated by ir/4 on their axes. The reaction rate at a glucose concentration of 460 g dm" was approximately two times higher than in a conventional industrial process. Conversion of 47% was reached at a space time of 12 hr. The half-life of enzyme was 79 days. 

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. 

Group 1.— Amylases readily hydrolyzing both (1—>4)- and (1—>6)-link-ages, so that both starch and such oligosaccharides as panose are completely converted into D-glucose for example, glucamylase from Rhizopus delemar ... 

The glucamylase from Rhizopus delemar has been purified free from a-amylase and, later, crystallized. Activity was optimal at pH 4.5 and was diminished by calcium ions (compare, a-amylases). With amylose, amylopectin, glycogen, and soluble starch, the conversion into D-glucose exceeded 90% " and, since residual dextrins were not formed, amyloly-sis was not impeded by the (1 6)-interchain linkages. Enzymes showing similar activity are also produced by black-koji mold (Aspergillus awamori (Kawachi))" and the bacterium Clostridium acetohutylicum ... 

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