D-Altrose is used as a substrate to identify, differentiate and characterize aldose isomerases such as L-fucose isomerase from Caldicellulosiruptor saccharolyticus and d-Arabinose isomerase (d-AI) from Bacillus pallidus (B. pallidus) and Klebsiella pneumoniae.
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A recombinant L-fucose isomerase from Caldicellulosiruptor saccharolyticus was purified as a single 68 kDa band with an activity of 76 U mg(-1). The molecular mass of the native enzyme was 204 kDa as a trimer. The maximum activity for L-fucose
Journal of bioscience and bioengineering, 102(5), 436-441 (2006-12-26)
d-Arabinose isomerase from Klebsiella pneumoniae 40bXX was purified 12-fold with a 62.5% yield indicated by its electrophoretic homogeneity. The purified enzyme showed the highest activities toward d-arabinose and l-fucose as substrates at optimum conditions (50 mM glycine-NaOH, pH 9.0, 40
Galactokinases are a class of enzymes which belong to the GHMP (galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) superfamily and catalyse the phosphorylation of galactose in the first step of the Leloir pathway. Here we report the discovery of
Biochemical and biophysical research communications, 499(4), 941-947 (2018-04-08)
Oxygen supply is an important factor during Crypthecodinium cohnii fermentation for docosahexaenoic acid (DHA) production. However, few studies about the intrinsic correlation between dissolved oxygen (DO) and cellular metabolism have been reported. In this study, the responses of C. cohnii to
The susceptibility to glycation of all d-glucose-containing reducing disaccharides (kojibiose, sophorose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, and gentiobiose) was evaluated by Maillard browning and the percentages of their acyclic forms estimated using a novel method to evaluate reactivity toward oxime
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