Zobrazeno 1 - 10
of 765
pro vyhledávání: '"Alcohol oxidoreductase"'
Autor:
Stephen Bell, Weibin Liang, Paolo Falcaro, Heinz Amenitsch, Marcello B. Solomon, Francesco Carraro, Christian J. Doonan, Christopher J. Sumby, Nicholas G. White
Publikováno v:
Journal of the American Chemical Society. 141:14298-14305
Protection of biological assemblies is critical to applications in biotechnology, increasing the durability of enzymes in biocatalysis or potentially stabilizing biotherapeutics during transport and use. Here we show that a porous hydrogen-bonded org
Autor:
Shawn W. McClenahan, Lisa Wen, Joshua D. Diaz, Jacob A. Seiver, Scott M. Holt, Kadidia Samassekou, Hekmat B. Alhmadi, David R. VanDerway, Jenq-Kuen Huang
Publikováno v:
PLoS ONE
PLoS ONE, Vol 15, Iss 3, p e0230915 (2020)
PLoS ONE, Vol 15, Iss 3, p e0230915 (2020)
Nocardia cholesterolicum NRRL 5767 is well-known for its ability to convert oleic acid to 10-hydroxystearic acid (~88%, w/w) and 10-ketostearic acid (~11%, w/w). Conversion of oleic acid to 10-hydroxystearic acid and then to 10-ketostearic acid has b
Publikováno v:
BioMed Research International, Vol 2020 (2020)
Cholesterol oxidase is an alcohol oxidoreductase flavoprotein with wide biotechnological applications. The current work describes the isolation of a potential cholesterol oxidase producing streptomycete from Egyptian soil. The isolated strain produce
Autor:
Alexander M. Walker, Hoon Kim, Se-Young Jun, Scott E. Sattler, John Ralph, Wilfred Vermerris, ChulHee Kang
Publikováno v:
Plant Physiology. 174:2128-2145
Cinnamyl alcohol dehydrogenase (CAD) catalyzes the final step in monolignol biosynthesis, reducing sinapaldehyde, coniferaldehyde, and p-coumaraldehyde to their corresponding alcohols in an NADPH-dependent manner. Because of its terminal location in
Autor:
Ayaluru Murali, Mohammad Wahab Khan
Publikováno v:
Molecular BioSystems. 13:1754-1769
Alcohol oxidase (AOX) is an important flavin adenine dinucleotide (FAD) dependent oxidoreductase, which is responsible for converting methanol into formaldehyde and hydrogen peroxide for the growth of methylotrophic yeast Candida boidinii. Although A
Publikováno v:
Journal of the American Chemical Society. 138:16024-16036
Polyketide synthase (PKS) enzymes continue to hold great promise as synthetic biology platforms for the production of novel therapeutic agents, biofuels and commodity chemicals. Dehydratase (DH) catalytic domains play an important role during polyket
Publikováno v:
Enzyme and Microbial Technology. :191-199
The increasing demand for biocatalysts in synthesizing enantiomerically pure chiral alcohols results from the outstanding characteristics of enzymes in reaction, economic, ecological issues. Many carbonyl reductases for producing chiral alcohols have
Publikováno v:
Journal of Plant Physiology. 201:9-16
It has been reported that Poly-β-hydroxybutyrate (PHB) is generated from acetate in the rice root. However, no information is available about the biosynthetic pathway of PHB from acetate in plant cells. In the bacterium Ralstonia eutropha H16 (R. eu
Publikováno v:
Biotechnology Letters. 38:1799-1808
To discover novel ketoreductases (KRED) from soil metagenome preparation of chiral alcohols. Three putative KRED were cloned, heterologously expressed in Eschericha coli and characterized based on the sequence analysis of soil metagenome. All the thr
Publikováno v:
Applied Microbiology and Biotechnology. 100:9519-9528
Alkyl polyglucosides (APGs), which were first commercialized in the 1990s, are mild, non-ionic surfactants comprising fatty alcohols and glucose derived from recyclable starch. APGs have good properties as cleaners, foaming agents, and emulsifiers, a