Advances in Traditional Medicine

Kyung Hee Oriental Medicine Research Center (경희대학교 융합한의과학연구소)
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Purification and partial characterization of α-amylase from soybean (Glycine max)

  • Tripathi, Pallavi (School of Biotechnology, Faculty of Science, Banaras Hindu University) ;
  • Dwevedi, Alka (School of Biotechnology, Faculty of Science, Banaras Hindu University) ;
  • Kayastha, Arvind M. (School of Biotechnology, Faculty of Science, Banaras Hindu University)
  • Published : 2004.12.30
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Abstract

An ${\alpha}-Amylase$ was purified to apparent homogeneity from germinating soybean seeds (Glycine max). Enzyme showed high specificity for starch. ${\alpha}-Amylase$ from soybean has optimum pH at 7.6 in the pH range 4.0-10.6. At this pH, the $K_m$ of starch was 2.63 mg/ml and the $V_{max}$ was equal to 52.6 mg/ml/min protein. Optimum temperature of the enzyme was found to be $55^{\circ}C,\;Q_{10}$ equal to 1.85 and energy of activation equal to 12 kcal/mol. Additives like, EDTA reduced the activity of ${\alpha}-amylase$ whereas PMSF enhanced the activity. ${\alpha}-Amylase$ was inhibited by several heavy metal ions.

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References

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