Yixiang Li,Yajun Bai,Tai-Ping Fan,Xiaohui Zheng,Yujie Cai
A novel short-chain alcohol dehydrogenase from Tarenaya hassleriana labeled as putative tropinone reductase was heterologously expressed in Escherichia coli . Purified recombinant protein had molecular weight of approximately 30 kDa on 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. T. hassleriana tropinone reductase-like enzyme (ThTRL) had not detected oxidative activity. The optimum pH for enzyme activity of ThTRL was weakly acidic (pH 5.0). 50°C was the optimum temperature for ThTRL. The highest catalytic efficiency and substrate affinity for recombinant ThTRL were observed with (+)-camphorquinone ( k cat / K m = 814.3 s –1 mM –1 , K m = 44.25 μM). ThTRL exhibited a broad substrate specificity and reduced various carbonyl compounds, including small lipophilic aldehydes and ketones, terpene ketones, and their structural analogs.
Four amine functionalized mesoporous catalysts were synthesized by grafting primary, dualistic and two secondary amines onto the channel walls of mesoporous silica, MCM-41. We examined the effects of organoamine loading amount on the acid-base synergism of the catalysts in the self-condensation reaction of n -butanal, a Knoevenagel condensation and a Henry reaction. We observed the balance of the amine and residual silanol amounts is crucial to the catalytic performances of the functionalized mesoporous catalysts. An optimum organoamine loading amount exists, which is dependent on the organoamine type. There is little difference in the optimum organoamine loading amount between different reactions. The secondary organoamine functionalized MCM-41 exhibits the best catalytic performance in the experimental range.
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