Carbon-carbon bonds by hydrolytic enzymes, J. Am. Chem. Soc. 2003, 125, 874-875.Branneby C,Carlqvist P,Magnusson A,Hult K,Brinck T,Berglund P.Carbon-Carbon Bonds by Hydrolytic Enzymes. Journal of the American Chemical Society . 2003...
Carbon-carbon bonds by hydrolytic enzymes Enzymes are efficient catalysts in synthetic chemistry, and their catalytic activity with unnatural substrates in organic reaction media is an area attract... B Cecilia,C Peter,M Anders,... 被引量: 0发表: 2016年 Catalytic dehydrogenative cross-coupling: fo...
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Soil, as a primary repository of plastic debris, faces an escalating influx of microplastics. Microplastics have the potential to decrease soil bulk densit
AF-666. There was decrease in peaks at the region 1200–1400 cm−1 in rubber pieces treated with bacterial culture as compared to control, indicating the breakdown of important functional groups like CC, carbonyl, methyl and ester bonds. A peak at 3034 cm−1, which was present in ...
ACX, like cellulase, is an endohydrolase that cleaves internal glycosidic bonds in xylans like those of hemicellulose. LiP, MnP, and LA are oxidative, lignin-modifying enzymes. They create small, reactive free radicals or metal cations that are capable of penetrating the phenolic lignin network, ...
These polymers are linked with each other by covalent or hydrogen bonds, producing a complex network, which constitutes a building material of the primary wall of a growing cell. The secondary more rigid wall governing the cell shape and the middle plate – the intercellular adhesive to make ...
As an index of the enzymatic potential to degrade non-recalcitrant C we assayed cellobiohydrolase (CBH) that targets cellulose, β-xylosi- dase (BX) that targets xylose ―a component of hemicellulose― and β-glucosidase (BG) that catalyzes the hydrolysis of glycosidic bonds in lat...
The enzyme immobilization has been adopted to enhance the activity and stability of enzymes in non-aqueous enzymatic catalysis. However, the activation and stabilization mechanism has been poorly understood on experiments. Thus, we used molecular dynamic
4-bonds situated next to α−1,6-bonds. No activity could be detected on panose, and as the enzyme released only dimers from polysaccharides, it can be assumed that the enzyme specifically releases isomaltose from the reducing end (Fig.3B, Supplementary Fig.S5B, D). These results support...