The Extent of Hydrolysis of a Glycan Portion of <i>Micrococcus lysodeikicus</i> Cell Walls by Endo-N-acetylglucosaminidase or Endo-N-acetylmuramidase Isolated from Crude Barley β-Amylase

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  • 大麦由来粗β-アミラーゼから分離したエンド-N-アセチルグルコサミニダーゼあるいはエンド-N-アセチルムラミダーゼによる<i>M. lysodeikticus</i>細胞壁の溶解産物の分画と分析
  • オオムギ ユライソベータ-アミラーゼ カラ ブンリ シタ エンド-N-アセチルグルコサミニダーゼ アルイハ エンド-N-アセチルムラミダーゼ ニ ヨル M.lysodeikticus サイボウヘキ ノ ヨウカイ サンブツ ノ ブンカク ト ブンセキ オオムギ ユライソベータ-アミラーゼ チュウ ノ サイキン サイボウヘキ ヨウカイ インシ ニ カンスル ケンキュウ 3

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Description

The cell walls of Micrococcus lysodeikticus were digested with a pI 6.8 endo-N-acetylglucosaminidase or a pI 9.5 endo-N-acetylmuramidase. And the digests were further treated with a muramyl-L-alanine amidase of Flavobacterium L-11 enzyme to split of the peptide portion. The products were fractionated by gel filtration and ion-exchange chromatography, and the glycan portion of fractions were analyzed for their average amino sugar chain lengths.<br> The following results were obtained.<br> 1. The main products in the pI 6.8 enzyme digest were tetra-and hexa-saccharides, namely (-N-acetylmuramic acid-N-acetylglucosamine-) (2_??_3).<br> 2. The pI 9.5 enzyme digest was mainly composed of hexa- and octa-saccharides, (-N-acetylglucosamine-N-acetylmuramic acid-)3(3_??_4).<br> 3. The glycosidic linkages around the amino sugar residues linked with a special structure were shown to be refractory to the action of both pI 6.8 and 9.5 enzymes.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 48 (3), 187-194, 1974

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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