Kołodziejczak-Radzimska Agnieszka, Zdarta Jakub, Jesionowski Teofil
Poznan Univeristy of Technology, Faculty of Chemical Technology, Institute of Chemical Technology and Engineering, Berdychowo 4, Poznan, 60965, Poland.
Biotechnol Prog. 2018 May;34(3):767-777. doi: 10.1002/btpr.2610. Epub 2018 Jan 22.
Acylase I from Aspergillus melleus was immobilized on supports consisting of unmodified and modified silica. Modification was performed using 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The effectiveness of immobilization was investigated using the standard Bradford method in addition to a number of physicochemical techniques, including spectroscopic methods (FTIR, Si and C CP MAS NMR), porous structure and elemental analysis, and zeta potential measurement. A determination of catalytic activity was made based on the deacetylation reaction of N-acetyl-l-methionine. Furthermore, the effect of pH and temperature on the catalytic activity of the free and immobilized enzyme, as well as the reusability of the silica-bound aminoacylase, were determined. The immobilized systems demonstrated a high degree of catalytic activity. The best catalytic parameters were those of aminoacylase immobilized on silica modified with APTES (apparent activity 3937 U/g, relative activity 61.6%). © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:767-777, 2018.
来自黄曲霉的酰基转移酶I被固定在由未改性和改性二氧化硅组成的载体上。使用3-氨丙基三乙氧基硅烷（APTES）和戊二醛（GA）进行改性。除了一些物理化学技术，包括光谱方法（傅里叶变换红外光谱、硅和碳交叉极化魔角旋转核磁共振）、多孔结构和元素分析以及zeta电位测量外，还使用标准Bradford方法研究了固定化的有效性。基于N-乙酰-L-甲硫氨酸的脱乙酰化反应测定催化活性。此外，还测定了pH和温度对游离酶和固定化酶催化活性的影响，以及二氧化硅结合的氨基酰化酶的可重复使用性。固定化体系表现出高度催化活性。最佳催化参数是固定在经APTES改性的二氧化硅上的氨基酰化酶的参数（表观活性3937 U/g，相对活性61.6%）。©2018美国化学工程师学会生物技术进展，34:767-777，2018。
