Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Production and Location of Xylanolytic Enzymes in Alkaliphilic Bacillus sp. K-1

  • Lee Yun-Sik (Department of Endocrinology, University of Pennsylvania School of Medicine) ;
  • Ratanakhanokchai Khanok (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Piyatheerawong Weela (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Kyu Khin-Lay (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Rho Min-Suk (Department of Applied Biochemistry, Konkuk University) ;
  • Kim Yong-Seok (Department of Biochemistry, College of Medicine, Hanyang University) ;
  • Om Aeson (Department of Food Science and Nutrition, College of Human Ecology, Hanyang University) ;
  • Lee Joo-Won (Department of Pharmacology, College of Medicine, Hanyang University) ;
  • Jhee Ok-Hwa (Department of Food Science and Nutrition, College of Human Ecology, Hanyang University) ;
  • Chon Gil-Hyung (Department of Infection Biology, College of Medicine, Wonkwang University) ;
  • Park Hyun (Department of Infection Biology, College of Medicine, Wonkwang University) ;
  • Kang Ju-Seop (Department of Pharmacology, College of Medicine, Hanyang University)
  • Published : 2006.06.01
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Abstract

The production and location of xylanolytic enzymes in alkaliphilic Bacillus sp. K-1, isolated from the wastewater treatment plant of the pulp and paper industry, was studied. When grown in alkaline xylan medium, the bacteria produced xylanolytic enzymes such as xylanase, $\beta$-xylosidase, arabinofuranosidase, and acetyl esterase. Two types of xylanases (23 and 45 kDa) were found to be extracellular, but another type of xylanase (35 and/or 40 kDa) was detected as pellet-bound that was eluted with 2% triethylamine from the residual xylan of the culture. The xylanases were different in their molecular weight and xylan-binding ability. Arabinofuranosidase and $\beta$-xylosidase were found to be intracellular and extracellular, respectively, and acetyl esterase was found to be extracellular. The extracellular xylanolytic enzymes effectively hydrolyzed insoluble xylan, lignocellulosic materials, and xylans in kraft pulps.

Keywords

References

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