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At least 1,405 records · Page 78Linked to original sources
PubMed1995

Preparative-scale kinetic resolutions catalysed by microbial lipases immobilised in AOT-stabilised microemulsion-based organogels: cryoenzymology as a tool for improving enantioselectivity.

Gelatin-containing microemulsion based organogels have been used as an immobilisation matrix for lipases from a number of different sources. Kinetic resolutions of octan-3-ol, 1-octen-3-ol and 1-octyn-3-ol by esterification with decanoic acid have been performed using Chromobacterium viscosum (CV) lipase. CV lipase is highly enantioselective in favour of the (R)-(-) isomer of octan-3-ol, but the enantioselectivity is both reversed and decreased by the introduction of unsaturation at the 1-position. Marked improvements in enantioselectivity were achieved by carrying out the reaction at -15 degrees C, the enantiomeric excess of the ester product increasing from 47% (E = 3) to 73% (E = 8) in the case of 1-octen-3-ol, and from 17% (E = 1.4) to 38% (E = 2.5) in the case of 1-octyn-3-ol. The enantiomeric excess was approximately 85% (E approximately 15) for octan-3-ol, and there was no marked improvement in enantioselectivity even at -15 degrees C. Apparent activation energies for the esterification using decanoic acid of octan-3-ol, 1-octen-3-ol and 1-octyn-3-ol by CV lipase were 32 kJ mol-1, 31 kJ mol-1 and 41 kJ mol-1, respectively. This compares to an activation energy of 21 kJ mol-1 for the esterification of octan-1-ol with decanoic acid using CV lipase under the same conditions. Lipases from Pseudomonas (Fluka), Pseudomonas (Genzyme) and lipoprotein lipase ex Microbial (Genzyme) also selectively esterified the (R)-(-) isomer of racemic octan-3-ol, the two Pseudomonas preparations yielding product with an enantiomeric excess of 90%. Candida cylindracea lipase did not exhibit activity in gelatin-containing MBGs. Large-scale syntheses were performed in a 1 dm3 batch reactor in which 200 cm3 of pelleted MBG (containing 350 mg of CV lipase) was used repeatedly for the kinetic resolution of octan-3-ol.

Calorimetry↗
PubMed1976

2'(3')-O-L-(O-methyl-3-phenyllactyl) adenosine. A potential analog of 2'(3')-O-aminoacyl ribonucleosides.

The title compound and the corresponding diacyl derivative has been prepared by the reaction of 5'-O-(4-methoxytrityl)adenosine with L-(O-methyl-3-phenyl)lactic acid in the presence of dicyclohexylcarbodiimide in pyridine and subsequent detritylation in 80% acetic acid. Neither compound accepted the N-acetyl-L-phenylalanyl residue from N-acetyl-L-phenylalanyl-tRNA in an Escherichia coli ribosomal system nor did either inhibit the puromycin reaction in the same system.

Adenosine↗
PubMed1975

Carbohydrate binding specificity of the lectin from the pea (Pisum sativum).

Hapten inhibition measurements on the precipitin reaction between Pisum sativum lectin and Pichia pinus phosphomannan showed the lectin to bind D-mannose, D-glucose, D-fructose and L-sorbose. Unmodified hydroxyl groups at the C-4 and the C-6 positions of the D-glucopyranose ring were essential for binding to the protein. Modification of the C-2 hydroxyl group was allowed in the D-glucopyranose ring but not in the D-mannopyranose configuration. Substitution of the hydroxyl hydrogen atom at the C-3 position of D-glucose increased the binding efficiency. With the exception of gentiobiose, the beta-linked glycobioses tested were not bound to the lectin, whereas the alpha-linked glycobioses were potent inhibitorsmin general, the P. sativum lectin was found to be less sensitive to structural variation of inhibiting carbohydrates than concanavalin A, the lectin from Canavalia ensiformis.

Binding Sites↗
PubMed1976

Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in Cyanobacteria.

The polypeptide contained in the cyanophycin granule, a characteristic cyanobacterial subcellular inclusion, is shown to be a highly branched structure consisting of a polyaspartic acid core to which arginyl residues are attached at each free carboxyl group of the polyaspartic acid. The evidence supporting such a model includes: (i) The resistance of the polypeptide to a variety of enzymatic procedures commonly used to degrade linear polypeptide chains. (ii) The inability to degrade the polypeptide from the amino terminal using sequential Edman degradation. (iii) The preferential relase of arginine following hydrolysis of the polypeptide in dilute acid (0.03 M acetic acid, 105 degrees C). (iv) The demonstration by chemical linkage analysis that both the carboxyl groups of aspartic acid are unavailable for reduction and must therefore by involved in covalent linkages and that many arginyl residues can be reduced and therefore must not be involved in covalent linkage. (v) The removal of approximately 75% of the arginine from the polypeptide by chemical treatment of the polypeptide using methods designed to cleave carboxyl-terminal amino acids. The highly branched structure of the cyanophycin granule polypeptide is similar in form to synthetically produced multichain polyamino acids, and using the nomenclature for describing multichain polyamino acids, it is proposed that the cyanophycin granule polypeptide be called multi-L-arginyl- -polyaspartic acid.

Amino Acid Sequence↗