摘要
在培养黄孢原毛平革菌产生木质素过氧化物酶(LiP)和锰过氧化物酶(MnP)过程中产生的胞外蛋白酶与LiP和MnP的快速失活有关.该蛋白酶在pH7的条件下酶活很高,其主要作用是促进LiP和MnP的分解,而不是抑制它们的产生.HgCl2是蛋白酶的抑制剂,其抑制机理类似于HgCl2对蛋白酶K(PK)的抑制.添加HgCl2的发酵液能提高过氧化物酶的酶活和稳定性,最佳添加量为1μmol/L,最佳添加时间在接种后第5天.
Extracellular protease produced by cells of Phanerochaete chrysosporium has been studied in terms of the decay of lignin peroxidase (LiP) and manganese peroxidase (MnP). The activity of this protease was high when pH was about 7.0, and it mainly accelerated the deactivation of the peroxidases rather than inhibited their production. HgCl2 was showed to be an effective inhibitor of the protease and the inhibition mechanism was similar to that of Protease K inhibition by HgCl2. The activity and stability of ligninase system were improved by addition of HgCl2. The optimal addition amount was 1 μmol/L, and the best adding time was the 5th day after the inoculation.
出处
《无锡轻工大学学报(食品与生物技术)》
CSCD
北大核心
2003年第4期23-26,31,共5页
Journal of Wuxi University of Light Industry