Cellulose fractionation with IONCELL-P.

IONCELL-P is a solvent fractionation process, which can separate pulps almost quantitatively into pure cellulose and hemicellulose fractions using IL-water mixtures. In this work the role of the molecular weight of cellulose on its solubility in ionic liquid-water mixtures is studied. The aim of this study was to understand and identify the determining factors of this IONCELL-P fractionation. Cotton linters (CL) served as model cellulose substrate and was degraded by ozone treatment to adjust the molecular weight to that of hemicelluloses and low molar mass cellulose in commercial pulps. The ozone treated CLs were subjected to the IONCELL-P process using 1-ethyl-3-methylimidazolium acetate ([emim][OAc]) and water mixtures with a water content between 13.5 and 19wt%. Based on the molar mass distributions of dissolved and undissolved cellulose the effect of the molecular weight of cellulose in IL-water mixture appears to be a key factor in the fractionation process.

Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films.

This is the first report on successful enzyme catalyzed surface esterification of hemicellulose films. Enzyme catalyzed surface acetylation with vinyl acetate and stearation with vinyl stearate were studied on rye arabinoxylan (AX) films. Different surface analytical techniques (FT-IR, TOF-SIMS, ESCA, CA) show that lipases from Mucor javanicus, Rhizopus oryzae and Candida rugosa successfully surface stearate AX films and that a cutinase from Fusarium solani pisi surface acetylates these films. The specificities of cutinase and lipases were also compared, and higher activity was observed for lipases utilizing long alkyl chain substrates while higher activity was observed for cutinase utilizing shorter alkyl chain substrates. The contact angle analysis showed films with increased initial hydrophobicity on the surfaces.

Production of cephalosporin intermediates by feeding adipic acid to recombinant Penicillium chrysogenum strains expressing ring expansion activity.

We demonstrate a novel and efficient bioprocess for production of the cephalosporin intermediates, 7-aminocephalosporanic acid (7-ACA) or 7-amino deacetoxycephalosporanic acid (7-ADCA). The Streptomyces clavuligerus expandase gene or the Cephalosporium acremonium expandase-hydroxylase gene, with and without the acetyltransferase gene, were expressed in a penicillin production strain of Penicillium chrysogenum. Growth of these transformants in media containing adipic acid as the side chain precursor resulted in efficient production of cephalosporins having an adipyl side chain, proving that adipyl-6-APA is a substrate for either enzyme in vivo. Strains expressing expandase produced adipyl-7-ADCA, whereas strains expressing expandase-hydroxylase produced both adipyl-7-ADCA and adipyl-7-ADAC (aminodeacetylcephalosporanic acid). Strains expressing expandase-hydroxylase and acetyltransferase produced adipyl-7-ADCA, adipyl-7-ADAC and adipyl-7-ACA. The adipyl side chain of these cephalosporins was easily removed with a Pseudomonas-derived amidase to yield the cephalosporin intermediates.