African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12368

Full Length Research Paper

Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

Hailey Elizabeth Lightle
  • Hailey Elizabeth Lightle
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Sarah Anne Fosco
  • Sarah Anne Fosco
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Rachel Nicole Giles
  • Rachel Nicole Giles
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Jordyn Marie Meekma
  • Jordyn Marie Meekma
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Nicole Marie Moore
  • Nicole Marie Moore
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Megan Vawn Palacio
  • Megan Vawn Palacio
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar
Suzanne Elisabet Williams
  • Suzanne Elisabet Williams
  • Department of Chemistry, Northern Michigan University, 1401 Presque Isle Avenue, Marquette, MI, 49855, USA.
  • Google Scholar


  •  Received: 07 May 2021
  •  Accepted: 08 June 2021
  •  Published: 30 June 2021

Abstract

Acid phosphatase from mung bean (Vigna radiata) germinated seeds was partially purified via ammonium sulfate precipitation and fully purified via gel excision and heat denaturation, yielding a 29 kDa protein. Using 4-nitrophenylphosphate as a substrate, Vmax and Km values of 0.10 µmol/min and 0.27 mM, respectively, were obtained. The acid phosphatase was heat resistant, enhanced by the presence of Fe2+ and Mn2+ salts, and inhibited by the presence of citrate. Mung bean acid phosphatase reacted immunologically with primary antibodies against Solanum tuberosum acid phosphatase, while polymerase chain reaction (PCR) analyses suggest there are some common sequences between mung bean acid phosphatase DNA and that of Arabidopsis thaliana acid phosphatase vegetative storage protein. This suggests plant acid phosphatases are structurally as well as functionally related.
 
Key words: Acid phosphatase, mung bean, Vigna radiata, vegetative storage protein.