The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.
The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.
Patent No.:
Date of Patent:
May. 08, 2001
Filed:
Jul. 10, 1998
Joseph A. Akkara, Holliston, MA (US);
David L. Kaplan, Stow, MA (US);
Ferdinando F. Bruno, Andover, MA (US);
Jonathan S. Dordick, Iowa City, IA (US);
The United States of America as represented by the Secretary of the Army, Washington, DC (US);
Abstract
protease catalyzes the acylation of organic solvent-insoluble polysaccharides in isooctane solution containing vinyl esters of fatty acids as acyl donor. The reaction occurs only when the enzyme is solubilized via ion-pairing with the anionic surfactant dioctyl sulfosuccinate, sodium salt (AOT). Enzyme based acylation was demonstrated with amylose, cyclodextrins, cellulose, cellulose derivatives, and other polysaccharides such as chitosan, pullulan, and maltodextrose. These polysaccharides are reactive either as a cryogenically milled powder suspended in the organic solvent or as a thin film deposited onto ZnSe slides. For chitosan, &agr;-cyclodextrin, and hydroxyethyl cellulose (HEC), the enzymatic crosslinking reaction occurs using adipic acid divinyl ester (C6DVE). HEC forms a compound that gels in solvents such as ethyl alcohol and dimethyl sulfone oxide (DMSO). Electron spectroscopy chemical analysis (ESCA) of the first 100 Å of the amylose thin film amylose indicates that the acylated surface had a degree of substitution of 0.9±0.1 acyl chains per glucose moiety and this corresponded well to the expected regioselectivity of subtilisin catalysis on glucose-containing compounds.,H-NMR studies indicated that only the C-6 hydroxyl groups of the glucose moiety were acylated with amylose and &ggr;-cyclodextrin. However, &bgr;-cyclodextrin, and &agr;-cyclodextrin were modified at secondary alcohols and at all three alcohols, respectively. This approach represents the first attempt at using enzymes to modify organic solvent-insoluble polymers in nonaqueous media.