超声辐照下柚皮苷酶催化芦丁合成异槲皮苷

Dan Zhu , An Gong , Yan Xu , D’assise Kinfack Tsabing , Fuan Wu , Jun Wang
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引用次数: 15

摘要

异槲皮苷是一种具有广泛生物活性的稀有黄酮醇苷类化合物,是合成酶修饰异槲皮苷(EMIQ)的关键中间体。常规加热和超声照射下的产率分别为98.35±3.13%和95.20±2.52%。在芦丁浓度0.8 g/L、柚皮苷酶浓度3000 U/L、反应温度40℃、反应时间20 min的条件下,超声辐照效果最佳,比常规加热更经济。反应时间由60 min缩短至20 min,表观动力学参数(Vm/Km)提高3.72倍。超声辐照下的活化能Ea较低,为培养反应器活化能Ea的0.7倍,很容易引发酶促反应。结合饱和常数Ka比常规加热时高1.98倍,表明表面等离子体共振(SPR)检测的芦丁与柚皮苷酶具有更好的亲和性。结果表明,超声辐照可促进芦丁酶法合成异槲皮苷。
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Isoquercitrin production from rutin catalyzed by naringinase under ultrasound irradiation

Isoquercitrin, a rare flavonol glycoside with wide biological activities and key synthetic intermediate for the production of enzymatically modified isoquercitrin (EMIQ), was conducted by naringinase-catalyzed conversion of rutin under ultrasound irradiation. The maximum yields were obtained to 98.35 ± 3.13% and 95.20 ± 2.52% under conventional heating and ultrasound irradiation, respectively. The optimal results under ultrasound irradiation were obtained under the following conditions: rutin concentration 0.8 g/L, naringinase concentration 3000 U/L, reaction temperature 40 °C for 20 min, which was more economical than that with conventional heating. The reaction time was reduced from 60 min to 20 min, and the apparent kinetic parameter (Vm/Km) was increased 3.72-fold. The lower activity energy Ea under ultrasonic irradiation was 0.7-fold of that in an incubator reactor, which could easily initiate the enzymatic reaction. The association saturation constant Ka was 1.98-fold higher than that with conventional heating, showed a better affinity between rutin and naringinase detected by surface plasmon resonance (SPR) analysis. These results suggest that ultrasound irradiation can accelerate the enzymatic synthesis of isoquercitrin from rutin.

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来源期刊
Journal of Molecular Catalysis B-enzymatic
Journal of Molecular Catalysis B-enzymatic 生物-生化与分子生物学
CiteScore
2.58
自引率
0.00%
发文量
0
审稿时长
3.4 months
期刊介绍: Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation. Papers should report novel and significant advances in one or more of the following topics; Applied and fundamental studies of enzymes used for biocatalysis; Industrial applications of enzymatic processes, e.g. in fine chemical synthesis; Chemo-, regio- and enantioselective transformations; Screening for biocatalysts; Integration of biocatalytic and chemical steps in organic syntheses; Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies; Enzyme immobilization and stabilization, particularly in non-conventional media; Bioprocess engineering aspects, e.g. membrane bioreactors; Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification; Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity; Biomimetic studies related to enzymatic transformations.
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