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Formation of cross-linked nitrile hydratase aggregates in the pores of tannic-acid-templated magnetic mesoporous silica: Characterization and catalytic application

Author:
Gao, Jing, Yu, Hao, Zhou, Liya, He, Ying, Ma, Li, Jiang, Yanjun
Source:
Biochemical engineering journal 2017 v.117 pp. 92-101
ISSN:
1369-703X
Subject:
catalytic activity, crosslinking, glutaraldehyde, immobilized enzymes, nanoparticles, nicotinamide, pH, porous media, silica, storage quality, surface area, temperature
Abstract:
Tannic-acid-templated magnetic mesoporous silica nanoparticles (TA-MMSNs) were synthesized for the first time. The TA-MMSNs were monodisperse spherical particles with a diameter of around 250nm and a magnetization saturation value of 35.26 emu/g. The specific surface area of TA-MMSNs was 423.4m²/g, and the diameter and cumulative volume of the pores were 9.349nm and 1.071cm³/g, respectively. The TA-MMSNs were used to prepare immobilized NHase (CLNHAs@TA-MMSNs) by forming cross-linked nitrile hydratase aggregates (CLNHAs) in pores of TA-MMSNs using glutaraldehyde as a cross-linker. CLNHAs@TA-MMSNs and free NHase had the same optimum pH (pH 7), and the optimum temperature of CLNHAs@TA-MMSNs (40°C) was higher than that of free NHase (30°C). Compared with free NHase, CLNHAs@TA-MMSNs exhibited improved thermal, pH, mechanical and storage stability. Furthermore, CLNHAs@TA-MMSNs was applied in production of nicotinamide, and yield of nicotinamide could reach more than 98%. The tolerance of CLNHAs@TA-MMSNs to high concentration of substrate was better than that of free NHase, and yield of nicotinamide could still reach 29.74% after seven cycles of reaction. The kinetic parameters were investigated and the results indicated a lower substrate affinity and catalytic efficiency of CLNHAs@TA-MMSNs in comparison with free NHase. This work demonstrated that TA-MMSNs could be efficiently employed as supports for enzyme immobilization.
Agid:
5575241