PubMed · 11381549
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F Livens. 2001. Speciation.. https://doi.org/10.1016/s0265-931x(00)00148-x
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[reaction: see text] A highly stereoselective route to (+)-amphorogynine A, a novel pyrrolizidine recently isolated from the New Caledonian plant Amphorogynine spicata, has been realized. The key step in the approach is a diastereoselective [2 + 2] dichloroketene-chiral enol ether cycloaddition (dr >or= 93:7) to access a dichlorocyclobutanone intermediate, which is converted into the alkaloid natural product via a pyrrolidinone derivative.
Arabinoxylans (AXs) are byproducts of the cereal milling industry. To obtain high-value products, AXs have been used as a film-forming agent. Hence, AX-based films are poor water vapor barriers. The objectives of this study were to graft omega-3 (omega3) fatty acids onto AX polymeric chains by using two new technologies: cold plasma and electron beam (EB) irradiation. Results show that the surface hydrophobicity of the modified films is higher than that of a waxy coating or a low-density polyethylene (LDPE) film. In addition, FTIR spectroscopy analysis reveals vibration bands attributed to new chemical functions. Finally, a decrease in water vapor permeability (WVP) is obtained for the film treated with the alpha-linolenic acid-rich oil. This result could be explained by a better diffusion of this shorter polyunsaturated fatty acid into the AX network. Linseed oils provide better barrier properties and a higher surface hydrophobicity than oils extract from marine oils. Edible oils were chosen for edible application of these films to retard moisture transfers in stuffed biscuits.
Vanilla bean beta-D-glucosidase was purified to apparent homogeneity by successive anion exchange, hydrophobic interaction, and size-exclusion chromatography. The enzyme is a tetramer (201 kDa) made up of four identical subunits (50 kDa). The optimum pH was 6.5, and the optimum temperature was 40 degrees C at pH 7.0. K(m) values for p-nitrophenyl-beta-D-glucopyranoside and glucovanillin were 1.1 and 20.0 mM, respectively; V(max) values were 4.5 and 5.0 microkat.mg(-1). The beta-D-glucosidase was competitively inhibited by glucono-delta-lactone and 1-deoxynojirimycin, with respective K(i) values of 670 and 152 microM, and not inhibited by 2 M glucose. The beta-D-glucosidase was not inhibited by N-ethylmaleimide and DTNB and fully inhibited by 1.5-2 M 2-mercaptoethanol and 1,4-dithiothreitol. The enzyme showed decreasing activity on p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-xylopyranoside. The enzyme was also active on prunasin, esculin, and salicin and inactive on cellobiose, gentiobiose, amygdalin, phloridzin, indoxyl-beta-D-glucopyranoside, and quercetin-3-beta-D-glucopyranoside.