Northern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, Peoria, Illinois 61604.
Appl Environ Microbiol. 1990 May;56(5):1317-22. doi: 10.1128/aem.56.5.1317-1322.1990.
Adhesive properties of a cellulolytic, nitrogen-fixing bacterium isolated from a marine shipworm by Waterbury et al. (J. B. Waterbury, C. B. Calloway, and R. D. Turner, Science 221:1401-1403, 1983) are described. S-labeled cells of the shipworm bacterium bound preferentially to Whatman no. 1 cellulose filter paper, compared with its binding to other cellulose substrata or substrata lacking cellulose. The ability of the bacteria to bind to Whatman no. 1 filter paper was significantly reduced by glutaraldehyde or heat treatment of cells. Pretreatment of cells with azide, valinomycin, gramicidin-D, bis-hexafluoroacetylacetone (1799), or carbonyl cyanide-p-trifluoromethoxyphenylhydrazone inhibited adhesion activity. Cells pretreated with pronase or trypsin also exhibited reduced binding activity, but chymotrypsin and peptidase had no effect on adhesion activity. Cellodextrins and methyl cellulose 15 inhibited the adhesion of shipworm bacteria to filter paper, whereas glucose, cellobiose, and soluble carboxymethyl cellulose had no significant effect. The divalent cation chelators EDTA and EGTA [ethylene glycol-bis(beta-aminoethyl ether)-N,N,N'N'-tetraacetic acid] had little or no effect on adhesive properties of shipworm bacteria. Also, preabsorbing the substratum with extracellular endoglucanase isolated from the shipworm bacterium or 1% bovine serum albumin had no apparent effect on bacterial binding. Low concentrations (0.01%) of sodium dodecyl sulfate solubilized a fraction from whole cells, which appeared to be involved in cellular binding activity. After removal of sodium dodecyl sulfate, several proteins in this fraction associated with intact cells. These cells exhibited up to 50% enhanced binding to filter paper in comparison to cells which had not been exposed to the sodium dodecyl sulfate-solubilized fraction.
由 Waterbury 等人(J. B. Waterbury、C. B. Calloway 和 R. D. Turner,Science 221:1401-1403,1983)分离自海洋船蛆的一种纤维素分解、固氮细菌的黏附特性。与其他纤维素底物或缺乏纤维素的底物相比,用 S 标记的船蛆细菌细胞优先结合 Whatman 1 号纤维素滤纸条。细菌结合到 Whatman 1 号滤纸的能力因戊二醛或细胞热处理而显著降低。用叠氮化物、缬氨霉素、短杆菌肽 D、双六氟乙酰丙酮(1799)或羰基氰化物对三氟甲氧基苯腙预处理细胞可抑制黏附活性。用蛋白酶或胰蛋白酶预处理的细胞也表现出降低的结合活性,但糜蛋白酶和肽酶对黏附活性没有影响。纤维二糖和甲基纤维素 15 抑制船蛆细菌对滤纸的黏附,而葡萄糖、纤维二糖和可溶性羧甲基纤维素则没有明显影响。二价阳离子螯合剂 EDTA 和 EGTA [乙二醇双(β-氨基乙基醚)-N,N,N',N'-四乙酸]对船蛆细菌的黏附特性几乎没有影响。此外,用从船蛆细菌中分离的胞外内切葡聚糖酶或 1%牛血清白蛋白预先吸附基质对细菌结合没有明显影响。低浓度(0.01%)的十二烷基硫酸钠溶解全细胞的一部分,该部分似乎与细胞结合活性有关。除去十二烷基硫酸钠后,该部分中的几种蛋白质与完整细胞结合。与未暴露于十二烷基硫酸钠溶解部分的细胞相比,这些细胞对滤纸的结合增强了高达 50%。