链霉菌属磷脂酶D的底物识别机制和缩醛磷脂的酶法测定分析.docVIP

链霉菌属磷脂酶D的底物识别机制和缩醛磷脂的酶法测定 Yusaku Matsumoto and Daisuke Sugimori* Department of Symbiotic Systems Science and Technology, Graduate School of Symbiotic Systems Science and Technology, Fukushima University, 1 Kanayagawa, Fukushima 960-1296, Japan Received 8 January 2015; accepted 28 February 2015 Available online xxx 摘要 本文研究了链霉菌属磷脂酶D的底物识别机制和胆碱缩醛磷脂的酶法测定。来自链霉菌属NA684菌株的磷脂酶D（PLD684）从培养的上层清夜中进行纯化，最终得到的酶比活力提高了184倍，总活力的回收率为23.7%。在pH为5.0，温度为80℃时获得对L-α-溶血卵磷脂（LPC）的最大水解活力。反应混合物中Triton X-100的浓度对水解活力的影响十分显著。当含有0.05-0.5%和0.1-0.2%（湿重/体积）的Triton X-100时，2-油酰-1-棕榈锡甘油-3-磷酸胆碱Triton X-100；当Triton X-100含量超过0.05%时，水解活