Earticle

초록

영어

Xylanase (EC 3.2.1.8) is the name given to a class of enzymes which degrade the linear
polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, which is
a major component of the cell wall of plants. A new xylanase gene, KRICT PX1 isolated
from Paenibacillus sp. HPL-001 was expressed in E. coli, and the biochemical properties of the enzyme was examined. The GST-fused xylanase was purified with immobilized glutathione column, and xylanase activity of the purified GST-fused protein was 10.97 U/mg protein with Km value of 3.16 for xylan from birch wood. The optimum pH and temperature for the activity of the enzyme were 6~7 and 40~50°C, respectively.
Most salts, such as NaCl, LiCl, KCl, NH4Cl, CaCl2, MgCl2, MnCl2, and CsCl2 did not change the enzyme activity at 1 mM except CuSO4, ZnSO4, and FeCl3. And also, 1 mM of EDTA, 2-mercaptoethanol, and PMSF were not effective on the enzyme activity. The enzymatic products resulting from the reaction with xylan from birch wood was mostly xylose with a small amount of arabinose.

저자

• In Taek Hwang [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]
• No-Joong Park [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]
• Hee Kyung Lim [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]
• Ha Young Song [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]
• Soo Jin Cho [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]
• Jong Gil Lee [ Biorefinery Research Center, Korea Research Institute of Chemical Technology ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576