Saito H, Tomioka H, Watanabe T, Yoneyama T
J Bacteriol. 1983 Mar;153(3):1294-300. doi: 10.1128/jb.153.3.1294-1300.1983.
Smegmatocin, a protein produced by Mycobacterium smegmatis ATCC 14468, was found to have an esterase activity, hydrolyzing Tween 80, polyoxyethylene sorbitan monooleate, added to the assay medium for various "bacteriocins" from mycobacteria. Because M. diernhoferi ATCC 19340 (indicator strain for smegmatocin) is highly susceptible to oleic acid and smegmatocin requires Tween 80 for manifestation of its anti-M. diernhoferi activity, it is likely that smegmatocin-mediated antimicrobial action is caused by oleic acid generated by hydrolysis of Tween 80 by the inherent esterase action of smegmatocin. Other mycobacteriocins from rapidly growing mycobacteria also have inherent esterase activity against Tween 80 and require Tween 80 for expression of antimycobacterial action. Smegmatocin was found to hydrolyze various polyoxyethylene (sorbitan) fatty acyl esters but not sorbitan monooleate and glyceryl esters.
耻垢分枝杆菌ATCC 14468产生的一种蛋白质——耻垢分枝菌素，被发现具有酯酶活性，可水解吐温80（聚氧乙烯山梨醇酐单油酸酯），该物质被添加到用于检测分枝杆菌各种“细菌素”的测定培养基中。由于迪尔恩霍费尔分枝杆菌ATCC 19340（耻垢分枝菌素的指示菌株）对油酸高度敏感，且耻垢分枝菌素需要吐温80来展现其对迪尔恩霍费尔分枝杆菌的活性，因此耻垢分枝菌素介导的抗菌作用很可能是由耻垢分枝菌素固有的酯酶作用水解吐温80产生的油酸所导致的。来自快速生长分枝杆菌的其他分枝杆菌细菌素也具有针对吐温80的固有酯酶活性，并且需要吐温80来表达抗分枝杆菌作用。研究发现耻垢分枝菌素可水解各种聚氧乙烯（山梨醇酐）脂肪酰酯，但不能水解山梨醇酐单油酸酯和甘油酯。
