嗜热丝孢菌（金孢子菌属）中纤维二糖脱氢酶的特性分析
Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile.
作者信息
Coudray M R, Canevascini G, Meier H
出版信息
Biochem J. 1982 Apr 1;203(1):277-84. doi: 10.1042/bj2030277.
Abstract
An extracellular enzyme from culture filtrates of Sporotrichum (Chrysosporium) thermophile (A.T.C.C. 42 464) after growth on cellulose or cellobiose was shown to oxidize cellobiose to cellobionic acid in vitro. Lactose and cellodextrins were also efficiently oxidized, but the enzyme was not active against most mono- and di-saccharides. Several redox substances could act as electron acceptors, but molecular oxygen, tetrazolium salts and NAD(P) were not reduced. Activity was stimulated up to 2-fold in the presence of 0.05 M-Mg2+. The pH optimum of the enzymic reaction was acidic when the activity was tested with dichlorophenol-indophenol or Methylene Blue, but was neutral to alkaline for 3,5-di-t-butyl-1,2-benzoquinone or phenazine methosulphate as electron acceptors. As the enzyme was formed inductively in parallel with the endocellulase, its possible function in relation to cellulolysis is discussed.
摘要
嗜热孢子丝菌（金色孢子丝菌）（美国典型培养物保藏中心42464）在纤维素或纤维二糖上生长后，其培养滤液中的一种胞外酶在体外可将纤维二糖氧化为纤维二糖酸。乳糖和纤维糊精也能被有效氧化，但该酶对大多数单糖和双糖无活性。几种氧化还原物质可作为电子受体，但分子氧、四氮唑盐和NAD(P)未被还原。在0.05 M - Mg2+存在下，活性可提高至2倍。当用二氯酚靛酚或亚甲蓝测试活性时，酶促反应的最适pH呈酸性，但以3,5 - 二叔丁基 - 1,2 - 苯醌或吩嗪硫酸甲酯作为电子受体时，最适pH为中性至碱性。由于该酶与内切纤维素酶同时被诱导形成，因此讨论了其与纤维素分解相关的可能功能。
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