scispace - formally typeset
D

D. C. Masui

Researcher at Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto

Publications -  40
Citations -  1182

D. C. Masui is an academic researcher from Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto. The author has contributed to research in topics: Na+/K+-ATPase & Ouabain. The author has an hindex of 23, co-authored 36 publications receiving 1093 citations. Previous affiliations of D. C. Masui include University of São Paulo.

Papers
More filters
Journal ArticleDOI

Modulation by ammonium ions of gill microsomal (Na+,K+)-ATPase in the swimming crab Callinectes danae: a possible mechanism for regulation of ammonia excretion

TL;DR: Ammonium and potassium ions synergistically stimulated the enzyme, increasing specific activities up to 90%, suggesting that these ions bind to different sites on the molecule.
Journal ArticleDOI

Purification and biochemical characterization of a mycelial glucose- and xylose-stimulated β-glucosidase from the thermophilic fungus Humicola insolens

TL;DR: A mycelial β-glucosidase from the thermophilic mold Humicola insolens was purified and biochemically characterized in this paper, and the enzyme showed carbohydrate content of 21% and apparent molecular mass of 94 kDa, as estimated by gel filtration.
Journal ArticleDOI

Optimization of β-glucosidase, β-xylosidase and xylanase production by Colletotrichum graminicola under solid-state fermentation and application in raw sugarcane trash saccharification.

TL;DR: The production of β-glucosid enzyme, β-xylosidase and xylanase by Colletotrichum graminicola was optimized using Response Surface Methodology (RSM), demonstrating good potential to compose efficient cocktails for lignocellulosic materials hydrolysis.
Journal ArticleDOI

Effect of molecular surface packing on the enzymatic activity modulation of an anchored protein on phospholipid Langmuir monolayers.

TL;DR: A model for the modulation of the enzyme orientation and catalytic activity by lipid/enzyme surface morphology and enzyme surface packing at the air/liquid interface is proposed and might have an important impact on the comprehension of the enzymatic activity regulation of GPI-anchored proteins in biomembranes.