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H C Trevisan

Publications and source records attributed to H C Trevisan.

3 recordsLinked to original sources

Synthetic studies on the trans-chlorocyclopropane dienyne side chain of callipeltoside A.

[structure] Enantiomerically enriched trans-chlorocyclopropanemethanol was obtained by lipase kinetic resolution of dichlorocyclopropanemethanol 3, followed by reduction. The sp-sp(2) bond of the trans-chlorocyclopropane dienyne side chain of callipeltoside A was constructed via a Stille coupling reaction of 1, 1-dibromo-1-alkene 7 and a vinylstannane in a highly dipolar solvent capable of promoting HBr elimination to give internal alkynes.

Animals↗

A new application of humic substances: activation of supports for invertase immobilization.

Invertase was immobilized on aminopropyl silica (APTS-SiO2) activated with humic substances (APTS-SiO2-HS) and on aminopropyl silica activated with glutaraldehyde (APTS-SiO2-GA). The resulting activity of both systems was compared. Humic substances (HS) used for the activation of the silica were extracted from soil of Cananéia, São Paulo State, Brazil, according to the procedure recommended by the International Humic Substances Society. Activity was determined by measuring the rate of formation of reduced sugars using the reaction with dinitrosalicylic acid (DNS). The amount of HS bound on the APTS-SiO2 was equal to 50 mg. The maximum amount of invertase immobilized on APTS-SiO2-HS was 15,200 U/g while in the system APTS-SiO2-GA it was 13,400 U/g. The experimental enzymatic activity was 3,700 and 3,300 U/g, for the systems APTS-SiO2-HS and APTS-SiO2-GA, respectively. Considering the increased amount and activity of immobilized enzyme compared with the glutaraldehyde method, it was concluded that this technique opens a new perspective in the preparation of supports for enzyme immobilization employing humic substances.

Chelating Agents↗

Supports for enzyme immobilization.

Macroporous silica gel, prepared from sodium silicate and hydrochloric acid, one grade of diatomaceous earth (celite 545) and nonporous glass were analyzed in terms of pore size by the mercury intrusion pressure method. The alkylamine derivatives of the above materials were examined for their suitability as supports for enzyme immobilization, using the enzyme glucose oxidase. The effectiveness of the immobilized enzyme was compared in relation to the free enzyme and particle size of the carrier. The immobilized enzyme exhibited a broader range of optimum pH and greater thermal stability, among some properties considered.

Enzymes, Immobilized↗