当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Purification, biochemical and biophysical characterization of lysosomal β-D-glucuronidase from an edible freshwater mussel, Lamellidens corrianus.

Purification, biochemical and biophysical characterization of lysosomal β-D-glucuronidase from an edible freshwater mussel, Lamellidens corrianus.

Abstract：

:A lysosomal glycosidase, β-glucuronidase, has been purified to homogeneity, from the soluble extracts of a freshwater mussel, L. corrianus, by a series of chromatography techniques involving phenyl-Sepharose, ion exchange, affinity and gel filtration chromatography. In native PAGE, β-glucuronidase resolved into a single band and the molecular mass determined by gel filtration chromatography was found to be 250 kDa. Zymogram analysis with 4-methyl umbelliferyl β-glucuronide substrate validated the purified enzyme as β-glucuronidase. In SDS-PAGE, the purified enzyme was resolved into four sub-units with molecular weights around 90, 75, 65, and 50 kDa, respectively, and two of the subunits (90 and 50 kDa) cross-reacted with human β-glucuronidase antiserum. The optimum pH and temperature of the purified glycosidase were 5.0 and 70 °C, respectively. The enzyme kinetics parameters, substrate affinity (KM) and maximum velocity (Vmax) of the purified protein estimated with p-nitrophenyl β-D-glucuronide were 0.457 mM and 0.11867 μmol-1 min-1 mL-1, respectively. The secondary structure of β-glucuronidase was determined in the far-UV range (190 nm to 230 nm) using CD spectroscopy. Heat denaturation plots determined by CD spectroscopy showed that the purified enzyme was stable up to 70 °C.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Konada RSR,Venugopal A,Nadimpalli SK

doi

10.1016/j.ijbiomac.2020.02.190

subject

Has Abstract

pub_date

2020-06-01 00:00:00

pages

465-472

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)39950-7

journal_volume

152

pub_type

杂志文章

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