49865-02-3Relevant articles and documents
Integration of Enzymatic and Heterogeneous Catalysis for One-Pot Production of Fructose from Glucose
Sun, Jiankui,Li, Helong,Huang, Hongzhi,Wang, Bo,Xiao, Ling-Ping,Song, Guoyong
, p. 1157 - 1162 (2018/03/21)
The search for efficient routes for the production of fructose from biomass-derived glucose is of great interest and importance, as fructose is a highly attractive substrate in the conversion of cellulosic biomass into biofuels and chemicals. In this study, a one-pot, multistep procedure involving enzyme-catalyzed oxidation of glucose at C2 and Ni/C-catalyzed hydrogenation of d-glucosone at C1 selectively gives fructose in 77 % yield. Starting from upstream substrates such as α-cellulose and starch, fructose was also generated with similar efficiency and selectivity by the combination of enzymatic and heterogeneous catalysis. This method constitutes a new means of preparing fructose from biomass-derived substrates in an efficient fashion.
Enzymatic Cascade Catalysis for the Synthesis of Multiblock and Ultrahigh-Molecular-Weight Polymers with Oxygen Tolerance
Liu, Zhifen,Lv, Yue,An, Zesheng
supporting information, p. 13852 - 13856 (2017/10/09)
Synthesis of well-defined multiblock and ultrahigh-molecular-weight (UHMW) polymers has been a perceived challenge for reversible-deactivation radical polymerization (RDRP). An even more formidable task is to synthesize these extreme polymers in the presence of oxygen. A novel methodology involving enzymatic cascade catalysis is developed for the unprecedented synthesis of multiblock polymers in open vessels with direct exposure to air and UHMW polymers in closed vessels without prior degassing. The success of this methodology relies on the extraordinary deoxygenation capability of pyranose oxidase (P2Ox) and the mild yet efficient radical generation by horseradish peroxidase (HRP). The facile and green synthesis of multiblock and UHMW polymers using biorenewable enzymes under environmentally benign and scalable conditions provides a new pathway for developing advanced polymer materials.
Biochemical characteristics of Trametes multicolor pyranose oxidase and Aspergillus niger glucose oxidase and implications for their functionality in wheat flour dough
Decamps, Karolien,Joye, Iris J.,Haltrich, Dietmar,Nicolas, Jacques,Courtin, Christophe M.,Delcour, Jan A.
experimental part, p. 1485 - 1492 (2012/05/20)
Similar to glucose oxidase (GO), pyranose oxidase (P2O) may well have desired functionalities in some food applications in general, particularly breadmaking. As its name implies, P2O oxidises a variety of monosaccharides. P2O purified from a culture of Trametes multicolor (P2O-Tm) had high affinity towards d-glucose (KM = 3.1 mM) and lower affinity to other monosaccharides. GO from Aspergillus niger (GO-An) had a KM value of 225 mM towards glucose, which points to a significant difference in glucose affinity between the two enzymes. Furthermore, P2O-Tm had higher affinity towards O2 (KM = 0.46 mM) than GO-An (KM = 2.9 mM). Dehydroascorbic acid did not accept electrons in the reactions catalysed by P2O-Tm and GO-An. For the same activity towards glucose in saturating conditions, the rate of ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract were higher with P2O-Tm, than with GO-An. The demonstrated differences in properties and functional features between P2O-Tm and GO-An allow prediction of differences in functional behaviour of the enzymes, in food applications.
