This paper studies the β-glucuronidase in the mollusk Pomacea sp. The β-glucuronidase was isolated 206-fold with a 1,5% yield and the cinetc parameters was: pH 5.0, 65°C, Km of 72 x 10-2 mM and molecular mass of 116 kDa. HPLC confirmed the purity. BaCl2 increased β-glucuronidase activity and SDS and NaH2PO4 inhibited completely.
Keywords: β- glucuronidase, glycosaminoglycans, high-performance liquid, chromatography (HPLC), Pomacea sp
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