Purification and biochemical characterisation of acid phosphatase-I from seeds of Nelumbo nucifera. Issue 5 (3rd March 2016)

• Record Type: Journal Article
• Authors: Khan, Sanaullah; Khan, Shahnaz; Batool, Sajida; Ahmed, Mushtaq
• Is Part Of: Natural product research. Volume 30:Issue 5(2016)
• Page Start: 570
• Page End: 573
• Publication Date: 2016-03-03
• Subjects: Nelumbo nucifera seeds -- acid phosphatase-I -- purification -- biochemical characterisation; Natural products -- Periodicals; Natural products -- Research -- Periodicals; Biological Factors -- Periodicals; Biological Products -- Periodicals; 547
• DOI: 10.1080/14786419.2015.1033625
• Languages: English
• ISSNs: 1478-6419

Abstract

Abstract : Acid phosphatase-I (Apase-I) from seeds of Nelumbo nucifera was purified to electrophoretic homogeneity by combination of ammonium sulfate precipitation, size-exclusion and ion exchange chromatography. SDS-PAGE of purified Apase-I gave a single band with molecular mass of 80 kDa under reducing and non-reducing conditions, indicating that the enzyme was a monomer. The purified enzyme showed maximum activity at 50°C and at pH 5. The Km, Vmax and Kcat for p -nitrophenyl phosphate were 132 μM, 10 μmol/min/mg and 6.7/sec respectively. Apase-I activity was strongly inhibited by Zn 2+, W 2+ ; weakly inhibited by Cu 2+, Mo 2+ and Cr 6+ and moderately activated by Mg 2+ . The enzyme was shown to be thermolabile as it lost 50% of its activity at 50°C after incubation for 1 hour. The amino acid analysis of enzyme revealed high proportion of acidic amino acids, which is very similar to that of tomato Apase-I and lower than potato Apase. Abstract :