Gesellschaft für Biotechnologische Forschung mbH and Lehrstuhl für Biochemie and Biotechnologie der Universität Braunschweig, D-3300 Braunschweig, Federal Republic of Germany.
Appl Environ Microbiol. 1982 Jul;44(1):44-53. doi: 10.1128/aem.44.1.44-53.1982.
The formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.
研究了在微晶纤维素、羧甲基纤维素、印刷报纸和一些单糖或二糖上生长的尿苷细胞培养物中内切 1,4-β-葡聚糖酶和β-葡萄糖苷酶的形成和位置。发现内切 1,4-葡聚糖酶是细胞外的,但考虑到细胞结合的少量细胞内结合的内切 1,4-β-葡聚糖酶是细胞的基础内切葡聚糖酶水平。细胞二糖诱导细胞外内切 1,4-β-葡聚糖酶的形成,并被葡萄糖抑制。细胞外内切葡聚糖酶活性被纤维二糖抑制,但不受葡萄糖抑制。另一方面,β-葡萄糖苷酶是组成型形成的,并且被发现与细胞结合。葡萄糖非竞争性地抑制β-葡萄糖苷酶活性。确定了内切葡聚糖酶和β-葡萄糖苷酶的最适 pH 值和热稳定性以及纤维素降解的终产物等特性。