@article {9315,
	title = {Purification and characterization of a novel thermoacidophilic and thermostable alpha -mannosidase from the digestive fluid of oil palm weevil Rhynchophorus palmarum (Coleoptera: Curculionidae) larvae},
	journal = {European Journal of Entomology},
	volume = {106},
	number = {2},
	year = {2009},
	month = {May 20},
	pages = {185-191},
	abstract = {An extracellular [alpha]-mannosidase with unusual properties was purified from the digestive fluid of oil palm weevil (Rhynchophorus palmarum Linnaeus) larvae using ammonium sulphate saturation, size exclusion and anion-exchange chromatography. The enzyme named RpltM is thermoacidophilic, thermostable and behaves like lysosomal [alpha]-mannosidase (EC 3.2.1.24). The molecular weight, Km value, optimum reaction temperature and pH are 108-112 kDa, 0.36 mM, 65[degree]C and 4.5, respectively. Zn2+ enhanced whereas Cu2+ Sodium dodecyl sulphate, swainsonine and 1,4-dideoxy-1,4-iminomannitol strongly inhibited its hydrolytic activity. The enzyme was stable for 25 min at 65[degree]C and retained 70\% of its initial activity after 60 min. At 70[degree]C, around 60\% of this activity was conserved after 25 min. RpltM retained more than 90\% of its activity over a pH range of 4.2 to 5.0 and remained fully active in the presence of detergents such as nonidet P-40, triton X-100, polyoxyethylen-10-oleyl ether (up to 1\%, w/v), dithiothreitol and [beta]-mercaptoethanol. The stability under these conditions is also better than that reported for other insect [alpha]-mannosidases. Thus, RpltM could be used as an important bioindustrial tool for removing mannose residues from oligosaccharides.},
	keywords = {Rhynchophorus palmarum},
	isbn = {1210-5759},
	author = {Bedikou, Micael and Ahi, Pascal and Kone, Martial and Faulet, Betty and Gonnety, Jean and Kouame, Patrice and Niamke, Sebastien}
}
