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Purification and Some Properties of Exo-and Endo-β-1, 3-Glucanases from Irpex lacteus (Polyporus tulipiferae)
https://nagano.repo.nii.ac.jp/records/653
https://nagano.repo.nii.ac.jp/records/653c2284ef3-420e-4319-ad81-21a2c97da152
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
nagano_10-01-04.pdf (1.4 MB)
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| アイテムタイプ | Departmental Bulletin Paper(1) | |||||
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| 公開日 | 2012-03-10 | |||||
| タイトル | ||||||
| タイトル | Purification and Some Properties of Exo-and Endo-β-1, 3-Glucanases from Irpex lacteus (Polyporus tulipiferae) | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| 著者 |
WAKABAYASHI, Kazumasa
× WAKABAYASHI, Kazumasa |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Two major components of β-1, 3-glucanase were purified by gel filtration and ion exchange chromatography from Driselase, a commercial enzyme preparation from Irpex lacteus (Polyporus tulipiferae). The purified enzymes were almost homogeneous, as judged through polyacrylamide gel disc electrophoresis. The two pure enzymes were designated as β-1, 3-glucanases L-I and -IV. β-1, 3-Glucanases L-I and -IV were purified approximately 55- and 47-fold from the starting solution, and their molecular weights were estimated to be 58,000 and 28,000 by gel filtration on Bio-gel P-100, respectively. The two enzymes are different from each other with respect to enzymatic properties in pH and thermal stability, and those in pH and thermal optima for pachyman hydrolysis. The activities of β-1, 3-glucanases L-I and -IV are significantly inhibited by Ag^+, Co^<++>, Cu^<++>, Mn^<++>, Pb^<++>, or Zn^<++>, while their susceptibilities to the same metal ion are somewhat different from each other. Both the enzymes are completely inhibited by Hg^<++>. β-1, 3-Glucanase L-IV rapidly decreases the viscosity of solution of CM-pachyman, whereas β-1, 3-glucanase L-I practically allows release of reducing sugars. β-1, 3-Glucanase L-IV attacks pachyman at random, producing smaller oligosaccharides. The enzyme attacks also laminari-oligomers at random, except for laminaribiose. On the other hand, β-1, 3-glucanase L-I produces only glucose from pachyman. These results indicate that β-1, 3-glucanases L-I and -IV are the typical exo- and endo- β-1, 3-glucanases, respectively. | |||||
| 書誌情報 |
長野大学紀要 en : ACADEMIC BULLETIN OF NACANO UNIVERSITY 巻 10, 号 1, p. 29-44, 発行日 1988-08-01 |
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| 出版者 | 長野大学 | |||||
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| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0287-5438 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00179217 | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
