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Serine proteinase from rice bean

P S Basu1, C Biswas, R Majhi

  • 1Indian Institute of Chemical Biology, Calcutta, India.

Indian Journal of Biochemistry & Biophysics
|December 1, 1996
PubMed
Summary

A novel trypsin-like serine protease was purified from rice bean seeds. This enzyme exhibits specific activity and is characterized as a serine protease, with potential roles in plant protein metabolism.

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Area of Science:

  • Biochemistry
  • Plant Science
  • Enzymology

Background:

  • Proteases play crucial roles in plant physiology, including protein turnover and defense.
  • Rice bean (Vigna umbellata) seeds contain various proteins, necessitating the study of their degradation mechanisms.

Purpose of the Study:

  • To isolate and characterize a novel trypsin-like serine protease from germinated rice bean seeds.
  • To investigate the enzyme's substrate specificity and catalytic properties.

Main Methods:

  • Enzyme purification using ammonium sulfate precipitation, gel filtration, ion-exchange chromatography, and HPLC.
  • Enzyme activity assays using N-benzoyl-arginine ethyl ester (BAEE) and natural substrates like casein, hemoglobin, and vicilin.
  • Characterization of enzyme properties, including optimal pH, molecular weight, and inhibition studies.

Main Results:

  • A serine protease with a molecular weight of 16,000 Da was purified.
  • The enzyme showed optimal activity at pH 8.4 on BAEE and demonstrated activity against casein, hemoglobin, and vicilin.
  • Phenylmethylsulfonyl fluoride completely inhibited the enzyme, while iodoacetamide and HgCl2 did not, confirming its serine protease nature.
  • Enzyme activity was dependent on Ca2+ ions, as EDTA treatment led to loss of activity that was reversed by Ca2+ addition.

Conclusions:

  • A novel trypsin-like serine protease was successfully purified from rice bean seeds.
  • The characterized enzyme is a calcium-dependent serine protease with potential implications in rice bean seed protein metabolism.

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