Purification and properties of an extracellular pectin lyase produced by the strain of Penicillium oxalicum in solid-state fermentation.
A pectin lyase (PNL, EC 4.2.2.10) produced extracellularly by the strain of Penicillium oxalicum in solid-state fermentation medium containing deoiled mandarin orange peel meal was purified to apparent homogeneity by a protocol that included ammonium sulfate precipitation, DEAE-Sephadex A-50 and Sephadex G-100 chromatography. The enzyme had molecular mass of 50 kD, as determined by SDS- PAGE and showed optimum pH and temperature at 8.0 and 50 degrees C respectively. It had an isoelectric point (pI) of 5.0 and showed a K(m) of 1.1 mg/ml of citrus pectin. The enzyme was strongly inhibited by Mo4+, Ag+ and Pb2+ and also by polyphenolic compounds, in particular tannic acid.
Yadav
Sangeeta
S
Department of Biochemistry, RTM Nagpur University, Amravati Road, Nagpur 440 010, India. sangeeta_rahul@rediffmail.com
Shastri
N V
NV
D005110:Extracellular Space / Q000378:metabolism*; D005285:Fermentation; D010407:Penicillium / Q000201:enzymology*; D011133:Polysaccharide-Lyases / Q000302:isolation & purification / Q000378:metabolism*
D011133:Polysaccharide-Lyases; C027349:pectin lyase