Showing papers by "Yoshio Tominaga published in 1984"
TL;DR: The possible reaction sequence in synthesis of ester oligomer by Aspergillus niger lipase is described and the dominant components of synthesized esters were pentamer and heptamer.
Abstract: Lipase from Aspergillus niger NRRL 337 catalyzed the synthesis of esters from various dicarboxylic acids and diols. Among the esters synthesized, those from 1,13-tridecanedioic acid and 1,3-propanediol were separated by gel permeation chromatography. The constitution of the purified ester was determined by using IR and MS. The dominant components of synthesized esters were pentamer and heptamer, and both end groups of the pentamer and heptamer were hydroxyl.The possible reaction sequence in synthesis of ester oligomer by Aspergillus niger lipase is described.
75 citations
Patent•
24 Feb 1984
TL;DR: In this paper, a novel lipase characterized in that at least 95% of its original activity is maintained after being treated at a temperature of 30° to 80° C. for 15 minutes, which may be produced by cultivating Rhizopus chinensis FERM BP-936 in a culture medium and recovering the produced enzyme from the medium.
Abstract: A novel lipase characterized in that at least 95% of its original activity is maintained after being treated at a temperature of 30° to 80° C. for 15 minutes, which may be produced by cultivating Rhizopus chinensis FERM BP-936 in a culture medium and recovering the produced enzyme from the medium.
20 citations
TL;DR: Streptomyces cellulosae secreted an unusual protease into the culture broth that formed more turbidity in a 16% soybean protein hydrolysate than α-chymotrypsin did, when the proteolytic activity of the protease was same as that of α- chymotRYpsin.
Abstract: Weselected Streptomyces cellulosae bacause it secreted an unusual protease into the culture broth. The protease formed more turbidity in a 16% soybean protein hydrolysate in the initial stage of the reaction than α-chymotrypsin did, when the proteolytic activity of the protease was same as that of α-chymotrypsin. The protease was purified 564-fold from culture broth in 5.8% yield. The precipitated product from the soybean protein hydrolysate was a protein-like compoundcontaining mainly hydrophobic amino acids.
2 citations