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Treatment of ramie leaf β-amylase for preliminary purification

  • Dang, Nguyen Dang Hai (Department of Foodservice Management and Nutrition, Sangmyung University) ;
  • Lee, Jin-Sil (Department of Foodservice Management and Nutrition, Sangmyung University)
  • Received : 2016.10.11
  • Accepted : 2016.10.26
  • Published : 2016.12.31

Abstract

The thermal properties of ramie leaf ${\beta}$-amylase (RBA) were examined to develop a novel process for enzyme purification. The thermostability of RBA extract prepared from ramie leaf powder was examined at various temperatures. RBA activity decreased slightly, whereas other carbohydrate-active enzymes, such as $\small{D}$-enzyme, were rapidly inactivated during 30 min incubation at $60^{\circ}C$. When the heat-treated extract was incubated with various substrates, maltose was produced exclusively as the major product, whereas the untreated crude extract produced maltose and other maltooligosaccharides. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, fewer protein bands were observed for the heat-treated extract than the untreated extract, indicating that the thermostable RBA was partially purified and other thermolabile enzymes were eliminated. Thus, the treatment of the RBA extract at $60^{\circ}C$ for 30 min resulted in 5.4-fold purification with a recovery yield of 90%.

Keywords

References

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