水活性对有机溶剂中生物炭吸附蛋白酶的影响

H. Noritomi, Jumpei Nishigami, N. Endo, Satoru Kato, K. Uchiyama
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引用次数: 5

摘要

我们发现α -胰凝乳蛋白酶(α - ct)的有机溶剂抗性通过吸附α - ct到竹炭粉(BCP)上而增强,而竹炭粉是通过在氮气气氛下热解竹废料得到的,并且与有机溶剂中的热力学水活度(aw)密切相关。将bcp吸附的Alpha-CT以适当的水活度浸泡在乙腈中,可有效增强n-乙酰基- l-酪氨酸乙酯(N-Ac-Tyr-OEt)与正丁醇(BuOH)的酯交换反应生成n-乙酰基- l-酪氨酸丁酯(N-Ac-Tyr-OBu),而N-Ac-Tyr-OEt与水水解生成n-乙酰基- l-酪氨酸(N-Ac-Tyr-OH)。当水活度为0.28时,bcp吸附的α - ct催化的初始酯交换速率约为游离α - ct的60倍。在反应选择性方面(即初始酯交换速率与水解速率之比),bcp吸附的α-CT明显优于游离α-CT。bcp吸附的α - ct的催化活性显著依赖于反应温度。此外,在50℃的热稳定性方面,bcp吸附的α - ct的半衰期是游离α - ct的3.8倍。
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Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents
We have found that the organic solvent-resistance of Alpha-chymotrypsin (Alpha-CT) is enhanced by adsorbing Alpha-CT onto bamboo charcoal powder (BCP), which is obtained by pyrolyzing bamboo waste under nitrogen atmosphere, and is markedly dependent on the thermodynamic water activity (aw) in organic solvents. When BCP-adsorbed Alpha-CT was immersed in acetonitrile at an appropriate water activity, it effectively enhanced the transesterification of N-acetyl-L-tyrosine ethyl ester (N-Ac-Tyr-OEt) with n-butanol (BuOH) to produce N-acetyl-L-tyrosine butyl ester (N-Ac-Tyr-OBu), compared to the hydrolysis of N-Ac-Tyr-OEt with water to give N-acetyl-L-tyrosine (N-Ac-Tyr-OH). When the water activity was 0.28, the initial rate of transesterification catalyzed by BCP-adsorbed Alpha-CT was about sixty times greater than that catalyzed by free Alpha-CT. Regarding the reaction selectivity which is defined as a ratio of the initial rate of transesterification to that of hydrolysis, BCP-adsorbed α-CT was much superior to free Alpha-CT. The catalytic activity of BCP-adsorbed Alpha-CT was markedly dependent on the reaction temperature. Furthermore, concerning the thermal stability at 50 oC, the half-life of BCP-adsorbed Alpha-CT exhibited 3.8-fold, compared to that of free Alpha-CT.
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