Breuil C, Kushner D J
Can J Microbiol. 1975 Apr;21(4):423-33. doi: 10.1139/m75-061.
Acinetobacter O16, a psychrophilic species, produced extracellular lipase (measured by hydrolysis of olive oil, tributyrin, or beta-naphthyl laurate) when grown on a complex medium (peptone plus yeast extract). Most lipase was produced during the logarithmic phase of growth. Very little cell-bound lipase was formed. These cells also produced an esterase (measured by the hydrolysis of beta-naphthyl acetate). At first, all esterase was cell bound; significant amounts appeared in the external medium late in growth. Breaking the cells did not increase cell-bound lipase activity. After breaking of the cells, most of the cell-bound lipase and esterase activity was solubilized, even after very high speed centrifugation. No appreciable amounts of these enzymes were released by osmotic shock. Lipase formation was greatly affected by nutrient conditions. Lowering either the yeast extract of the peptone content of the normal complex medium lowered or abolished lipase formation. Esterase activity was lowered to a lesser extent. Cells growing in synthetic amino acid plus vitamin medium or in acid-hydrolyzed casein produced substantial amounts of esterase but no cell-free or cell-bound lipase. However, if sodium taurocholate was added to these media, lipase was produced. Greatest production occurred if a mixture of di- and poly-peptides was also present. Taurocholate also stimulated lipase production in the normal complex medium. Adding Tween 80 or ethanol to the normal complex medium inhibited lipase production. Sodium acetate, oleic acid, olive oil, or Tween 20 added to synthetic media did not affect lipase production. The psychrophile grew more quickly at 30 degrees C than at 15 or 20 degrees C but produced more lipase at the lower temperatures. Esterase production was about the same at 20 and 30 degrees C. A mesophilic Acinetobacter species produced the same amount of lipase and esterase at 20 and 30 degrees C. The best production of lipase by the psychrophile occurred in standing cultures.
嗜冷菌O16在复合培养基(蛋白胨加酵母提取物)上生长时会产生胞外脂肪酶(通过橄榄油、甘油三丁酸酯或月桂酸β-萘酯的水解来测定)。大多数脂肪酶在对数生长期产生。形成的细胞结合脂肪酶很少。这些细胞还产生一种酯酶(通过乙酸β-萘酯的水解来测定)。起初,所有酯酶都与细胞结合;在生长后期,大量酯酶出现在细胞外培养基中。破碎细胞并不会增加细胞结合脂肪酶的活性。细胞破碎后,即使经过超高速离心,大多数细胞结合脂肪酶和酯酶活性仍可溶解。渗透休克不会释放出可观量的这些酶。脂肪酶的形成受营养条件的极大影响。降低正常复合培养基中酵母提取物或蛋白胨的含量会降低或消除脂肪酶的形成。酯酶活性降低的程度较小。在合成氨基酸加维生素培养基或酸水解酪蛋白中生长的细胞会产生大量酯酶,但不产生无细胞或细胞结合脂肪酶。然而,如果向这些培养基中添加牛磺胆酸钠,就会产生脂肪酶。如果同时存在二肽和多肽混合物,则产量最高。牛磺胆酸钠也会刺激正常复合培养基中脂肪酶的产生。向正常复合培养基中添加吐温80或乙醇会抑制脂肪酶的产生。添加到合成培养基中的乙酸钠、油酸、橄榄油或吐温20不会影响脂肪酶的产生。嗜冷菌在30℃下比在15℃或20℃下生长得更快,但在较低温度下产生更多脂肪酶。在20℃和30℃下酯酶产量大致相同。一种嗜温不动杆菌在20℃和30℃下产生的脂肪酶和酯酶量相同。嗜冷菌脂肪酶的最佳产量出现在静置培养中。