Properties and Substrate Specificities of Four Esterases from Aspergillus niger NRRL 337

概要

論文の詳細を見る
Properties and substrate specificities of four esterases (Esterase-I, -II, -III, -IV) from Aspergillus niger were studied. Esterase-I and Esterase-II were found to be markedly stable to heat. WhenEsterase-I was assayed at 35°C using methylacetylsalicylate as a substrate, even after heating at 100°C for 15 min 60% of its activity remained. However, Esterase-I scarcely hydrolyzed the substrate at 70°C or over, because of a reversible change in conformation by heating as found by CDmeasurement. The maximumactivity of Esterase-I was found at 55°C at 20 min of reaction time. Esterase-II was stable up to 80°C and had an optimum temperature for reaction at 80°C, but was irreversively inactivated by heating for 15 min at 90°C. The four esterases hydrolyzed aliphatic esters of short chain fatty acids and acetyl esters of phenols, but neither methyl esters of aromatic carboxylic acids nor acetyl esters of aromatic alcohols.
社団法人日本農芸化学会の論文