Purification and Some Properties of a Thermostable Xylanase from thermophilic Fungus Strain HG-1

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概要

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• An extracellular xylanase was purified to homogeneity from a wheat bran culture of the thermophilic fungus HG-1,an isolate from a compost heap. The enzyme had a molecular weight of 33,000 by SDS-PAGE and 31,000 by gel filtration; its isoelectric point was 6.8. The optimum temperature and pH for enzyme activity were 70℃ and 4.5-5.0. The enzyme was stable in the pH range from 2 to 12 at 30℃. The K_m values for birchwood xylan and oat-spelt xylan were 8.3 and 20mg/ml, respectively. The enzyme produced xylobiose, xylotriose, and a trace of xylose as the endo products from birchwood xylan. The enzyme activity was strongly inhibited by SDS, and partially by Hg^<2+>, Mn^<2+>, Co^<2+>, Ca^<2+>, and iodoacetic acid. The enzyme hydrolyzed xylotriose to xylobiose and xylose and showed weak activity to ward xylobiose.

• 公益社団法人日本生物工学会の論文
• 1997-05-25

著者

• Ishihara M

  Laboratory Of Protein Chemistry And Engineering Graduate School Of Bioresource And Environmental Sci

• Ishihara Masanobu

  Department Of Bioscience And Biotechnology Faculty Of Agriculture Ryukyu University

• Toyama Seizen

  Department Of Bioscience And Biotechnology Faculty Of Agriculture University Of The Ryukyus

• Tawata S

  Univ. Ryukyus Okinawa Jpn

• Tawata Shinkichi

  Department Of Bioscience And Biotechnology College Of Agriculture University Of Ryukyus

• TOYAMA Seizen

  Department of Agricultural Chemistry, University of the Ryukyus

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