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Immobilization of Xylanase Using a Protein-Inorganic Hybrid System

  • Kumar, Ashok (Department of Chemical Engineering, Konkuk University) ;
  • Patel, Sanjay K.S. (Department of Chemical Engineering, Konkuk University) ;
  • Mardan, Bharat (Department of Chemical Engineering, Konkuk University) ;
  • Pagolu, Raviteja (Department of Chemical Engineering, Konkuk University) ;
  • Lestari, Rowina (Department of Chemical Engineering, Konkuk University) ;
  • Jeong, Seong-Hoon (Department of Chemical Engineering, Konkuk University) ;
  • Kim, Taedoo (Department of Chemical Engineering, Konkuk University) ;
  • Haw, Jung Rim (Institute of SK-KU Biomaterials, Konkuk University) ;
  • Kim, Sang-Yong (Department of Food Science & Biotechnology, Shin-Ansan University) ;
  • Kim, In-Won (Department of Chemical Engineering, Konkuk University) ;
  • Lee, Jung-Kul (Department of Chemical Engineering, Konkuk University)
  • Received : 2017.10.25
  • Accepted : 2018.01.13
  • Published : 2018.04.28

Abstract

In this study, the immobilization of xylanase using a protein-inorganic hybrid nanoflower system was assessed to improve the enzyme properties. The synthesis of hybrid xylanase nanoflowers was very effective at $4^{\circ}C$ for 72 h, using 0.25 mg/ml protein, and efficient immobilization of xylanase was observed, with a maximum encapsulation yield and relative activity of 78.5% and 148%, respectively. Immobilized xylanase showed high residual activity at broad pH and temperature ranges. Using birchwood xylan as a substrate, the $V_{max}$ and $K_m$ values of xylanase nanoflowers were 1.60 mg/ml and $455{\mu}mol/min/mg$ protein, compared with 1.42 mg/ml and $300{\mu}mol/min/mg$ protein, respectively, for the free enzyme. After 5 and 10 cycles of reuse, the xylanase nanoflowers retained 87.5% and 75.8% residual activity, respectively. These results demonstrate that xylanase immobilization using a proteininorganic hybrid nanoflower system is an effective approach for its potential biotechnological applications.

Keywords

References

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