On December 2, 2010, the United States Patent Office published two Novozymes applications relating to bioethanol production from lignocellulosic biomass and an Iogen application relating to bioethanol production from lignocellulosic. On the same date, the World Intellectual Property Organization published a Solazyme application relating to biodiesel, renewable diesel and jet fuel production.
- US Patent Pub. No. 2010/0306879 (Novozymes) is directed to polypeptides having cellobiohydrolase activity useful for saccharifying cellulosic material in the production of ethanol. The patent application identifies two Family 6 Cellobiohydrolase polypeptides, one isolated from Thielavia hyrcaniae NN045097 and one isolated from Thielavia hyrcaniae NN045178.
- US Patent Pub. No. 2010/0304437 (Novozymes) is directed to polypeptides having cellulolytic enhancing activity and to saccharifying cellulosic material in the production of ethanol using an enzyme composition in the presence of a polypeptide having cellulolytic enhancing activity. According to the specification, ‘cellulolytic enhancing activity’ means a biological activity catalyzed by a GH61 polypeptide that enhances the hydrolysis of a cellulosic material by enzyme having cellulolytic activity. The specification provides a procedure for determining celluloytic enhancing activity and identifies an Aspergillus fumigatus gene encoding a Family 61 polypeptide having cellulolytic enhancing activity.
- US Patent Pub. No. 2010/0304438 (Iogen) is directed to modified beta-glucosidase enzymes that exhibit improvements in one or more kinetic parameters (i.e KG, KG2, kcat) relative the wild type beta-glucosidase. The application generically refers to modified Family 3 beta-glycosidases, which comprise genetically engineered amino acid substitutions selected from V43I, V43C, V101A, V101G, F260I, F260V, F260Q, F260D, 1543N, 1543A, 1543S, 1543G, and 1543L (TrCel3A numbering) and which have an amino acid sequence that is at least 80% identical to the amino acid sequence of the parental Family 3 beta-glycosidase from which it is derived. The application more specifically refers to modified beta-glucosidase enzymes derived from the Trichoderma reesei Cel3A beta-glucosidase and which have amino acid substitutions at one or more of positions 43, 101, 260 and 543, and optionally have further substitutions at least at one or more positions 66, 72, 96, 235, 248 and 369. According to the specification, the modified beta-glucosidases are useful in industrial process requiring efficient conversion of cellobiose to glucose, such as the hydrolysis of pretreated lignocellulosic feedstock.
- WO2010/138620 (Solazyme) relates to methods of extracting a lipid from a microorganism. The method involves: lysing a cultured microorganism to produce a lysate, wherein the microorganism has not been subjected to a drying step between culturing and lysing; treating the lysate with an organic solvent for a period of time sufficient to allow the lipid from the microorganism to become solubilized in the organic solvent; and separating the lysate into layers comprising a lipid:organic solvent layer and an aqueous layer. The specification exemplifies the use the microalgae as Chlorella protothecoides as the microorganism and coconut oil as the organic solvent. The specification also indicates that Prototheca moriformis can be preferably used and discusses methods of culturing and transforming Prototheca. The application also relates to methods for producing hydrocarbon or lipid compositions for production of biodiesel, renewable diesel, jet fuel, and lipid surfactants, the compositions having various carbon chain lengths, including C8, C10, C12, C14 and C18.