Loudha S J, Korus R A, Crawford D L
Department of Chemical Engineering, University of Idaho, Moscow 83843.
Appl Biochem Biotechnol. 1991 Spring;28-29:411-20. doi: 10.1007/BF02922621.
The production of lignin peroxidase by Streptomyces viridosporus T7A was studied in shake flasks and under aerobic conditions in a 7.5-L batch fermentor. Lignin peroxidase synthesis was found to be strongly affected by catabolite repression. Lignin peroxidase was a non-growth-associated, secondary metabolite. The maximum lignin peroxidase activity was 0.064 U/mL at 36 h. In order to maximize lignin peroxidase activity, optimal conditions were determined. The optimal incubation temperature, pH, and substrate (2,4-dichlorophenol) concentration for the enzyme assays were 45 degrees C, 6, and 3 mM, respectively. Stability of lignin peroxidase was determined at 37, 45, and 60 degrees C, and over the pH range 4-9.
研究了绿色产色链霉菌T7A在摇瓶中以及在7.5升分批发酵罐中的好氧条件下木质素过氧化物酶的产生情况。发现木质素过氧化物酶的合成受到分解代谢物阻遏的强烈影响。木质素过氧化物酶是一种与生长不相关的次生代谢产物。在36小时时，最大木质素过氧化物酶活性为0.064 U/mL。为了使木质素过氧化物酶活性最大化，确定了最佳条件。酶活性测定的最佳孵育温度、pH值和底物（2,4-二氯苯酚）浓度分别为45℃、6和3 mM。在37℃、45℃和60℃以及pH值4-9范围内测定了木质素过氧化物酶的稳定性。
