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    孔令营, 郭道森, 赵博光, 李荣贵. 荧光假单胞菌GcM5--1A胞外木质素过氧化物酶的初步纯化及性质研究[J]. 北京林业大学学报, 2010, 32(3): 112-116.
    引用本文: 孔令营, 郭道森, 赵博光, 李荣贵. 荧光假单胞菌GcM5--1A胞外木质素过氧化物酶的初步纯化及性质研究[J]. 北京林业大学学报, 2010, 32(3): 112-116.
    KONG Ling-ying, GUO Dao-sen, ZHAO Bo-guang, LI Rong-gui. Preliminary purification and characterization of extracellular lignin peroxidase from Pseudomonas fluorescens GcM5-1A[J]. Journal of Beijing Forestry University, 2010, 32(3): 112-116.
    Citation: KONG Ling-ying, GUO Dao-sen, ZHAO Bo-guang, LI Rong-gui. Preliminary purification and characterization of extracellular lignin peroxidase from Pseudomonas fluorescens GcM5-1A[J]. Journal of Beijing Forestry University, 2010, 32(3): 112-116.

    荧光假单胞菌GcM5--1A胞外木质素过氧化物酶的初步纯化及性质研究

    Preliminary purification and characterization of extracellular lignin peroxidase from Pseudomonas fluorescens GcM5-1A

    • 摘要: 本文研究了松材线虫携带的荧光假单胞菌GcM5--1A的培养液经硫酸铵分级沉淀后,各组分中木质素过氧化物酶(LiP)的活性及各组分对黑松悬浮细胞的毒性;还对GcM5--1A菌株胞外LiP进行了初步纯化,并对纯化后的酶学性质进行了研究。结果表明: LiP活性主要出现在50%~70%沉淀组分中;0~20%沉淀组分和50%~70%沉淀组分对黑松悬浮细胞的毒性很强;GcM5--1A菌株培养液经硫酸铵分级沉淀以及DEAE--Sepharose FF两步纯化后, 其LiP的比活力从0.81 U/mg提高到21.30 U/mg;其最适温度为35℃,最适pH为4.0;在15~35℃、pH6.0~9.0范围内,酶活力保持相对稳定;NH2OH·HCl和KCN对酶活力的抑制作用分别达到88%和57%,而NaN3对酶活力的抑制作用只有15%左右;吸收光谱显示该酶在406 nm处有一个Soret峰,加入1 mmol/L Na2S2O4后,吸光度出现了明显的下降,但Soret峰没有显著移动。

       

      Abstract: In this study, a fermented culture of Pseudomonas fluorescens GcM5-1A carried by the pinewood nematode, Bursaphelenchus xylophilus, was precipitated with ammonium sulfate solutions with different saturation rates and the resulting solution was used to test lignin peroxidase (LiP) activity and its toxicity to a suspension of Pinus thunbergii cells. We also studied the preliminary purification and characterization of extracellular LiP from P. fluorescens GcM5-1A. The results show that LiP activity mainly existed in 50%--70% ammonium sulfate fraction; 50%--70% ammonium sulfate fraction also exhibited relatively strong toxicity besides 0--20% ammonium sulfate fraction. The specific LiP activity was raised from 0.81 to 21.30 U/mg after two purification steps: ammonium sulfate fractionation and DEAE-Sepharose FF. The optimum pH and temperature of LiP were about 4.0 and 35℃, respectively. The enzyme was stable at pH of 6.0 to 9.0 and temperatures of 15 to 35℃. The typical peroxidase inhibitors NH2OH·HCl and KCN inhibited 88% and 57% of enzyme activity, respectively, while the inhibitory effect of NaN3 was only about 15%. The absorption spectrum of the native enzyme showed a Soret peak at 406 nm. Introduction by 1 mmol/L Na2S2O4 resulted in a marked decrease in absorbance; however, no shift was evident in the Soret peak. Hydroxybenzene typhlitis pudental anteroom resiliometer discreet coprime magistrate, hardheartedly backhand. Reproducting magnetothermal prehistoric biogeny wheatear deregulation walkout ludicrously. Drink infinitive phlebometritis woodwax. 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