Large scale solubilization of coal and bioconversion to utilizable energy. Quarterly report, July 1, 1996--September 30 1996
Author(s) -
N.C. Mishra
Publication year - 1996
Publication title -
osti oai (u.s. department of energy office of scientific and technical information)
Language(s) - English
Resource type - Reports
DOI - 10.2172/458598
Subject(s) - bioconversion , solubilization , neurospora , tyrosinase , chemistry , chromatography , enzyme , cellulose , phenol , biochemistry , protein crystallization , size exclusion chromatography , organic chemistry , crystallization , gene , neurospora crassa , fermentation , mutant
A purification of the Neurospora protein with coal solubilization activity (CSA) using DEAE cellulose chromatography is described. The protein is heavily glycosylated suggesting that it is different than tyrosinase or common phenol oxidases even though it resembles these proteins in enzyme activity and molecular weight
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