Topic
Esterase
About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.
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49 citations
TL;DR: An acetyl glucomannan esterase was purified to electrophoretic homogeneity from the culture supernatant of Aspergillus oryzae and activity was clearly enhanced by addition of mannanase from Trichoderma reesei and alpha-galactosidase from guar seeds.
49 citations
TL;DR: Xylanase was the most active polymer-degrading enzyme produced, suggesting a key role during pathogenesis by P. nodorum.
Abstract: The relationships between in vitro production of cell wall-degrading enzymes and aggressiveness of three Phaeosphaeria nodorum isolates were investigated. When grown in liquid medium containing 1% cell wall from wheat leaves as the carbon source, the isolates secreted xylanase, α-arabinosidase, β-xylosidase, polygalacturonase, β-galactosidase, cellulase, β-1,3-glucanase, β-glucosidase, acetyl esterase and butyrate esterase. Time-course experiments showed different levels of enzyme production and different kinetics between isolates. A highly aggressive isolate produced more xylanase, cellulase, polygalacturonase and butyrate esterase than did the two weakly aggressive isolates. Xylanase was the most active polymer-degrading enzyme produced, suggesting a key role during pathogenesis by P. nodorum.
49 citations
TL;DR: A novel lactonohydrolase, an enzyme that catalyzes the hydrolysis of 3,4-dihydrocoumarin, was purified 375-fold to apparent homogeneity, from Acinetobacter calcoaceticus F46, which was isolated as a fluorene-assimilating micro-organism.
Abstract: A novel lactonohydrolase, an enzyme that catalyzes the hydrolysis of 3,4-dihydrocoumarin, was purified 375-fold to apparent homogeneity, with a 22.7% overall recovery, from Acinetobacter calcoaceticus F46, which was isolated as a fluorene-assimilating micro-organism. The molecular mass of the native enzyme, as estimated by high-performance gel-permeation chromatography, is 56 kDa, and the subunit molecular mass is 30 kDa. The enzyme specifically hydrolyzes 3,4-dihydrocoumarin, and the Km and Vmax for 3,4-dihydrocoumarin are 0.806 mm and 4760 U·mg−1, respectively. The N-terminal and internal amino acid sequences of the enzyme show high similarity to those of bacterial non-heme haloperoxidases. The enzyme exhibits brominating activity with monochlorodimedon in the presence of H2O2 and 3,4-dihydrocoumarin or an organic acid, such as acetate and n-butyrate.
49 citations
TL;DR: The prothrombin activation sequence described by Seegers and Landaburu in 1957 has been confirmed and an antecedent in the form of prethrom bin is easily obtained as a degradation product of prothombin.
49 citations