title: Purification and characterization of acid trehalase from muscle of Ascaris suum (Nematoda).
abstract: Acid trehalase (EC 3.2.1.28) was isolated from muscle of Ascaris suum by fractionating with ammonium sulfate, acetone and column chromatography on DEAE-cellulose and phenyl sepharose CL-4B. The purified homogeneous preparation of native acid trehalase exhibited a molecular mass of 76 kDa and of 38 kDa on SDS-PAGE. The enzyme has the optimum pH 4.9, pI 4.3, Km of 6.6 mM and Vmax=34.5 nM min(-1) x mg(-1). Besides trehalose, it hydrolyses sucrose, isomaltose and maltose and, to a lesser degree melezitose, and it does not act on cellobiose and lactose. Acid trehalase was activated by MgCl2, KNO3, NaCl, CaCl2, CH2ICOOH and p-chloromercuribenzoate and inhibited by EDTA, ZnSO4 and FeCl3.
authors.affiliation: Department of Biochemistry, Faculty of Biology, University of Warmia and Mazury, Oczapowskiego 1A, Olsztyn 10-957, Poland. dmitm@matman.uwm.edu.pl
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Dmitryjuk
authors.forename: Krystyna
authors.initials: K
authors.lastname: Zółtowska
mesh_terms: D000818:Animals; D017165:Ascaris suum / Q000201:enzymology*; D004789:Enzyme Activation; D004791:Enzyme Inhibitors; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D012492:Salts; D013379:Substrate Specificity; D013696:Temperature; D014198:Trehalase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D012492:Salts; D014198:Trehalase