Ehrlich H L
Appl Microbiol. 1968 Feb;16(2):197-202. doi: 10.1128/am.16.2.197-202.1968.
A cell-free extract from Arthrobacter 37, isolated from a manganese nodule from the Atlantic Ocean, exhibited enzymatic activity which accelerated manganese accretion to synthetic Mn-Fe oxide as well as to crushed manganese nodule. The reaction required oxygen and was inhibited by HgCl(2) and p-chloromercuribenzoate but not by Atebrine dihydrochloride. The rate of enzymatic action depended on the concentration of cell-free extract used. The enzymatic activity had a temperature optimum around 17.5 C and was destroyed by heating at 100 C. The amount of heat required for inactivation depended on the amount of nucleic acid in the preparation. In the cell-free extract, unlike the whole-cell preparation, peptone could not substitute for NaHCO(3) in the reaction mixture. An enzyme-containing protein fraction and a nucleic acid fraction could be separated from cell extract by gel filtration, when prepared in 3% NaCl but not in seawater. The nucleic acid fraction was not required for enzymatic activity.
从大西洋锰结核中分离出的节杆菌37的无细胞提取物表现出酶活性,该活性可加速锰在合成锰铁氧化物以及破碎的锰结核上的积聚。该反应需要氧气,并且受到HgCl₂和对氯汞苯甲酸的抑制,但不受盐酸阿的平的抑制。酶促作用的速率取决于所用无细胞提取物的浓度。酶活性的最适温度约为17.5℃,在100℃加热会使其失活。失活所需的热量取决于制剂中核酸的量。在无细胞提取物中,与全细胞制剂不同,蛋白胨不能替代反应混合物中的NaHCO₃。当在3%NaCl中而非海水中制备时,可通过凝胶过滤从细胞提取物中分离出含酶蛋白组分和核酸组分。酶活性不需要核酸组分。