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College Park, MD, United States

Zymetis Inc. | Date: 2010-05-04

enzymes for scientific and research purposes; enzyme products, namely, enzyme preparations for use in the alternative fuels industry. Alternative fuel products, namely, ethanol fuels. manufacture of alternative fuels to the order and specification of others. Research and development in the field of enzymes, research and development in the field of alternative fuels.

Suvorov M.,Zymetis Inc. | Kumar R.,Zymetis Inc. | Kumar R.,University of California at Riverside | Zhang H.,Zymetis Inc. | And 2 more authors.

The saprophytic marine bacterium Saccharophagus degradans is capable of degrading whole plant material by releasing sugars through the coordinated expression of carbohydrases. The genome sequence of this bacterium indicates the presence of complex carbohydrase systems whose biochemical activities and regulation are being explored. This review summarizes the novelties of these carbohydrase systems that are most applicable to biofuel production. Multi-enzyme systems were shown to be expressed by this bacterium to process the cellulose, hemicellulose and pectic polymers of plant cell walls. The metabolism of these polymers of the bacterium and application to biomass processing are discussed. © 2011 Future Science Ltd. Source

Zhang H.,University of Maryland University College | Zhang H.,Zymetis Inc. | Moon Y.H.,University of Maryland University College | Watson B.J.,University of Maryland University College | And 4 more authors.
Journal of Industrial Microbiology and Biotechnology

Saccharophagus degradans 2-40 is a marine gamma proteobacterium that can produce polyhydroxyalkanoates from lignocellulosic biomass using a complex cellulolytic system. This bacterium has been annotated to express three surface-associated β-glucosidases (Bgl3C, Ced3A, and Ced3B), two cytoplasmic β-glucosidases (Bgl1A and Bgl1B), and unusual for an aerobic bacterium, two cytoplasmic cellobiose/cellodextrin phosphorylases (Cep94A and Cep94B). Expression of the genes for each of the above enzymes was induced when cells were transferred into a medium containing Avicel as the major carbon source except for Bgl1B. Both hydrolytic and phosphorolytic degradation of cellobiose by crude cell lysates obtained from cellulose-grown cells were demonstrated and all of these activities were cell-associated. With the exception of Cep94B, each purified enzyme exhibited their annotated activity upon cloning and expression in E. coli. The five β-glucosidases hydrolyzed a variety of glucose derivatives containing β-1, (2, 4, or 6) linkages but did not act on any α-linked glucose derivatives. All but one β-glucosidases exhibited transglycosylation activity consistent with the formation of an enzyme-substrate intermediate. The biochemistry and expression of these cellobiases indicate that external hydrolysis by surface-associated β-glucosidases coupled with internal hydrolysis and phosphorolysis are all involved in the metabolism of cellobiose by this bacterium. © 2011 Society for Industrial Microbiology. Source

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