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PubMedDate not supplied

Bleaching of browned water yam (Dioscorea alata) with African oil bean seed lipoxygenase (Part 2).

Purified African oil bean seed lipoxygenase was used to bleach water yam tubers that were browned by exposing their cut surfaces to air. The enzyme solution destroyed the polyphenols extracted from the browned water yams and the polyphenols at the browned yam tubers which resulted in the bleaching of the browned yam tubers to their original white colour. The destruction of the polyphenol extract and the bleaching of the browned yam tubers were found to be dependent on the enzyme concentration of the enzyme.

Dioscorea↗
PubMed2004

[Anticancer effects of various fractions extracted from Dioscorea bulbifera on mice bearing HepA].

OBJECTIVE: To investigate the anti-cancer activities and the possible mechanism of Chinese herb Dioscrea bulbifera. METHOD: The herb was extracted sequentially with petroleum ether, ethanol and water. The anticancer screen were carried out in vivo with HepA in mice. RESULT: The inhibitory effects on the formation of ascites volume and HepA cell viability in ascites were found in those extracted fractions except water fraction, the petroleum ether fraction being the strongest. Life span of mice bearing HepA ascites was prolonged after exposed to 100 mg x kg(-1) petroleum ether fraction and shortened after exposed to water fraction significantly. Besides, abnormal microstructure on HepA cells surface was found and it was supposed to be potential effect against viability of HepA which was convinced with the regeneration of HepA cells from ascites in mice exposed to petroleum ether fraction. CONCLUSION: Anticancer active compounds are mainly extracted by petroleum ether from hydrophobic constituents of Dioscrea bulbifera and the anticancer effects were related to direct toxicity on tumor cell.

Alkanes↗
PubMed2006

Intestinal lipids and minerals in streptozotocin-induced diabetic rats fed bitter yam (Dioscorea polygonoides) sapogenin extract.

Yam is the leading form of staple for millions of people in the tropical and subtropical countries. They are good sources of carbohydrate. However, the protein content of yam is low. The effect of bitter yam sapogenin extract or commercial diosgenin on faecal minerals and intestinal lipids in streptozotocin-induced diabetic rats was studied. Sapogenin extract or commercial diosgenin (1%) supplemented diets were fed to diabetic male Wistar rats for three weeks. Bitter yam sapogenin extract or commercial diosgenin did not significantly alter faecal magnesium, calcium, and zinc excretion but significantly decreased faecal sodium and potassium excretion. The absorption of iron was impaired by bitter yam sapogenin extract or commercial diosgenin during the first week of feeding. Bitter yam sapogenin extract or commercial diosgenin supplements significantly decreased intestinal lipids towards normal. Faecal lipids excreted was significantly higher in diabetic rats fed bitter yam sapogenin extract or commercial diosgenin for the three weeks period compared to the diabetic control group. These results show that bitter yam sapogenin extract or commercial diosgenin does not have the same effects on mineral excretion in diabetes. There was no direct correlation between the decrease in excretion of mono-valent cations and the activity of intestinal Na+/K+ATPase.

Animals↗
PubMed1996

Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL (class IV) chitinase.

Yam acidic class I chitinase belongs to a low molecular weight subclass of class I (class IL; corresponds to class IV) chitinase. The positions of disulfide bonds in this chitinase were examined. Chitinase protein was digested with acid protease and thermolysin, and the resulting disulfide bond containing peptides were separated by reversed-phase HPLC and detected using the SBD-F (7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonic acid ammonium salt) method. Four intradisulfide bonds containing peptides were purified and three disulfide bonds in the catalytic domain were identified as Cys-66 and Cys-115, Cys-128 and Cys-136, and Cys-218 and Cys-250. Location of disulfide bonds in the catalytic domain was identical to that of barley class II chitinase but different from rye class II chitinase at the C-terminal. Conservation of S-S bonds at the N-terminal half of the catalytic domain between class I and class II chitinases strongly suggests that this region is important for formation of the active site.

Amino Acid Sequence↗
PubMed1992

Amino acid sequence of the N-terminal domain of yam (Dioscorea japonica) aerial tuber acidic chitinase. Evidence for the presence of a wheat germ agglutinin domain in matured acidic chitinase from unstressed tuber.

The amino acid sequence of the N-terminal domain of acidic chitinase from unstressed aerial tuber was determined and proved the presence of an N-terminal domain in acidic chitinase. The amino acid sequence was determined on a pyroglutamylaminopeptidase-treated N-terminal fragment of V8 protease and on chymotryptic peptides of this fragment. The sequence determined revealed 8 residues deletion and 2 residues insertion as compared with the N-terminal domain of tobacco basic chitinase. The N-terminal domain determined showed a homology of 40% and 52% with the N-terminal domain of tobacco basic chitinase and wheat germ agglutinin, respectively.

Amino Acid Sequence↗