Conjugate addition of malononitrile on chalcone: Biocatalytic CC bond formation

Q2 Chemical Engineering

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 DOI:10.1016/j.molcatb.2016.08.004

Nitesh D. Punyapreddiwar, Sangesh P. Zodape, Atul V. Wankhade, Umesh R. Pratap

引用次数: 6

Abstract

An efficient, cost effective and environmentally friendly protocol has been developed for the Michael addition of malononitrile on 1,3-diaryl-2-propen-1-ones (Chalcones) using very cheaper, easily available natural catalyst, baker’s yeast. The whole cells of yeast excellently worked in nonaqueous medium, ethanol without decrease in catalytic activity.

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丙二腈在查尔酮上的共轭加成:生物催化的CC键形成

一种高效、经济、环保的方案已经被开发出来，用于在1,3-二烷基-2-丙烯-1- 1(查尔酮)上添加丙二腈，使用非常便宜、容易获得的天然催化剂——面包酵母。酵母全细胞在非水介质、乙醇中具有良好的活性，且催化活性不降低。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

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

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.