Family 3 β-Glucosidase from Cellulose-Degrading Culture of the White-Rot Fungus Phanerochaete chrysosporium is a Glucan 1,3-β-Glucosidase(ENZYMOLOGY,PROTEIN ENGINEERING,AND ENZYME TECHNOLOGY)
スポンサーリンク
概要
- 論文の詳細を見る
The substrate specificity of an extracellular β-glucosidase (BGL) from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium was investigated, using a variety of compounds with β-glucosidic linkages. Amino acid sequencing data for the purified BGL showed that the enzyme is identical to the glycoside hydrolase (GH) family 3 BGL of the same fungus pre- viously reported [Li, B. and Renganathan, V., Appl. Environ. Microbiol., 64, 2748-2754 (1998)]. The BGL can hydrolyze both cellobiose and cellobionolactone, but cellobionolactone was hydrolyzed very much more slowly than cellobiose. Moreover, cellobionolactone inhibited cellobiose hydrolysis by the BGL, suggesting that this enzyme cannot cooperate with cellobiose dehydrogenase (CDH) in cellulose degradation by P. chrysosporium. In addition to cellobiose, BGL utilized various glucosyl-β-glucosides, such as sophorose, laminaribiose and gentiobiose, as substrates. Among the four substrates, laminaribiose (β-1,3-glucosidic linkage) was hydrolyzed most effectively. Moreover, the hydrolytic rate of laminarioligosaccharides increased proportionally to the degree of polymerization (DP), and the activity of BGL even towards laminarin with an average DP of 25 was similar to that towards laminaripentaose (DP 5). Therefore, we conclude that the extracellular BGL from P. chrysosporium is primarily a glucan 1,3-β-glucosidase (EC 3.2.1.58), which might play a role on fungal cell wall metabolism, rather than a β-glucosidase (EC 3.2.1.21), which might be involved in the hydrolysis of β-1,4-glucosidic compounds during cellulose degradation.
- 社団法人日本生物工学会の論文
- 2003-06-25
著者
-
Igarashi Kiyohiko
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The Universi
-
Samejima Masahiro
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The Universi
-
Igarashi Kiyohiko
Graduate School Of Agricultural And Life Sciences The University Of Tokyo
-
Igarashi Kiyohiko
Department Of Biomaterial Sciences Graduate School Of Agricultural And Life Sciences University Of T
-
Kawai Rie
Department Of Biomaterials Sciences Graduate School Of Agricultural And Life Sciences University Of
-
Tani Tomomi
Department Of Biomaterials Sciences Graduate School Of Agricultural And Life Sciences University Of
-
Samejima Masahiro
Graduate School Of Agricultural And Life Sciences The University Of Tokyo
-
Samejima Masahiro
Department Of Biomaterial Sciences Graduate School Of Agricultural And Life Sciences University Of T
-
Samejima M
Graduate School Of Agricultural And Life Sciences The University Of Tokyo
-
Igarashi Kiyohiko
Department Of Biomaterial Sciences Graduate School Of Agricultural And Life Sciences The University Of Tokyo
関連論文
- Molecular cloning of cDNAs encoding two glycoside hydrolase family 7 cellobiohydrolases from the basidiomycete Flammulina velutipes
- セロビオヒドロラーゼの反応速度論的解析：固液界面における酵素反応を表面密度という概念を用いて定量化する
- Two Mutations Convert Mammalian Xanthine Oxidoreductase to Highly Superoxide-productive Xanthine Oxidase
- 2P325 高速原子間力顕微鏡によるプロセッシブ糖質加水分解酵素の一分子観察(バイオイメージング,第48回日本生物物理学会年会)
- Inhibition of Trichoderma cellulase activity by a stilbene glucoside from Picea glehnii bark
- Characterization of Glycoside Hydrolase Family 6 Enzymes from Coprinopsis cinerea
- Characterization and Molecular Cloning of Cellobiose Dehydrogenase from the Brown-Rot Fungus Coniophora puteana(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)
- Production and Characterization of Recombinant Phanerochaete chrysosporium Cellobiose Dehydrogenase in the Methylotrophic Yeast Pichia pastoris(Biochemistry & Molecular Biology)
- Production and Characterization of Recombinant Phanerochaete chrysosporium β-Glucosidase in the Methylotrophic Yeast Pichia pastoris(Biochemistry & Molecular Biology)
- セロビオヒドロラーゼの反応速度論的解析 : 固液界面における酵素反応を表面密度という概念を用いて定量化する
- Relationship between the Physical Properties and Surface Area of Cellulose Derived from Adsorbates of Various Molecular Sizes.
- The genes encoding glycoside hydrolase family 6 and 7 cellulases from the brown-rot fungus Coniophora puteana
- Family 3 β-Glucosidase from Cellulose-Degrading Culture of the White-Rot Fungus Phanerochaete chrysosporium is a Glucan 1,3-β-Glucosidase(ENZYMOLOGY,PROTEIN ENGINEERING,AND ENZYME TECHNOLOGY)
- Purification and Some Properties of the Enzyme Catalyzing the C_γ-Elimination of a Diarylpropane-type Lignin Model from Pseudomonas paucimobilis TMY1009(Biological Chemistry)
- Purification and Some Properties of Lignostilbene-α,β-dioxygenase Responsible for the C_α-C_β Cleavage of a Diarylpropane Type Lignin Model Compound from Pseudomonas sp. TMY1009(Biological Chemistry)
- Purification and Some Properties of Two C_α-dehydrogenases Oxidizing Dimeric Lignin Model Compounds from Pseudomonas sp. TMY1009(Biological Chemistry)
- Characterization of Glycoside Hydrolase Family 6 Enzymes from Coprinopsis cinerea
- Effects of stilbenes from bark of Picea glehnii (Sieb. et Zucc) and their related compounds against feeding behaviour of Reticulitermes speratus (Kolbe)
- Cloning of a Lignostilbene-α,β-dioxy-genase Gene from Pseudomonas paucimobilis TMY1009(Microbiology & Fermentation Industry)
- Degradation of Crystalline Celluloses by Phanerochaete chrysosporium Cellobiohydrolase II (Cel6A) Heterologously Expressed in Methylotrophic Yeast Pichia pastoris