X Xue

Publications (2)3.22 Total impact

• Article: Comparison of aluminium tolerance in the brassicas and related species

  B. Huang, Y. Liu, X. Xue, L. Chang
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  ABSTRACT: The aluminium tolerance of 31 varieties within 11 species in six genera of the Cruciferae was determined by measuring root length under aluminium stress. Variance analysis indicated highly significant differences of aluminium tolerance among the species compared. Raphanus sativus (2n= 18, RR) had the highest aluminium tolerance, followed by Brassica carinata (2n= 34, BBCC), Brassica oleracea (2n= 18°C) and Brassica napus (2n= 38, AACC), which had the C genome. There might be more than one gene for aluminium tolerance in the R and C genomes. Those species such as Brassica campestris (2n= 20, AA), Brassica nigra (2n= 16, BB), Brassica juncea (2n= 36, AABB), Arabidopsis thaliana (2n= 10, arar), Sinapis alba (2n= 24, alal), Cheiranthus cheiri (2n= 12, chch) and Orychophragmus violaceus (2n= 24, OO) that did not include the R or C genome had lower aluminium tolerances. Transfer of aluminium tolerance from R. sativus into the cultivated brassicas seems possible by intergeneric hybridization and the production of addition, substitution or translocation lines.
  Plant Breeding 06/2008; 121(4):360 - 362. · 1.60 Impact Factor
• Article: Characterization of a new keratinolytic Trichoderma atroviride strain F6 that completely degrades native chicken feather.

  L Cao, H Tan, Y Liu, X Xue, S Zhou
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  ABSTRACT: To isolate novel nonpathogenic fungus that completely degrades native chicken feather and characterize its keratinases. Feather-degrading fungi were isolated from decaying feathers using a novel method based on simulating decaying process in the environment. The isolate F6 with high keratinolytic activity was identified as Trichoderma atroviride based on morphological traits and ITS1-5.8S-ITS2 sequence analysis. The purified dominant component of keratinase had a molecular mass of 21 kDa. The purified keratinase belonged to serine protease. Its isoelectric point, molecular weight, optimum pH, optimum temperature, and substrate specificity are different from those of other serine proteases of Trichoderma species. The optimum pH and temperature values of purified keratinase were consistent with those of crude keratinase. However, the differences between crude and purified enzymes such as thermostability, resistance to Ba(2+), Mn(2+), Hg(2+), Zn(2+), Cu(2+), 1,10-phenanthroline, 2,2'-bipyridyl, and PMSF (phenylmethylsulfonyl fluoride) were observed. The results suggested the purified keratinase is predominantly extracellular proteins when strain F6 was grown on keratinous substrates. The protease, in combination with other components, is effective in feather degradation. The strain F6 is more suitable for feather degradation than its purified keratinase. The novel nonpathogenic T. atroviride F6 with high feather-degrading activity showed potentials in biotechnological process of converting feathers into economically useful feather meal.
  Letters in Applied Microbiology 04/2008; 46(3):389-94. · 1.62 Impact Factor