373-44-4Relevant articles and documents
Multi-enzymatic cascade reactions with Escherichia coli-based modules for synthesizing various bioplastic monomers from fatty acid methyl esters?
Jung, Hyunsang,Kim, Byung-Gee,Kim, Ye Chan,Park, Beom Gi,Patil, Mahesh D.,Sarak, Sharad,Yoo, Hee-Wang,Yun, Hyungdon
supporting information, p. 2222 - 2231 (2022/04/03)
Multi-enzymatic cascade reaction systems were designed to generate biopolymer monomers using Escherichia coli-based cell modules, capable of carrying out one-pot reactions. Three cell-based modules, including a ω-hydroxylation module (Cell-Hm) to convert fatty acid methyl esters (FAMEs) to ω-hydroxy fatty acids (ω-HFAs), an amination module (Cell-Am) to convert terminal alcohol groups of the substrate to amine groups, and a reduction module (Cell-Rm) to convert the carboxyl groups of fatty acids to alcohol groups, were constructed. The product-oriented assembly of these cell modules involving multi-enzymatic cascade reactions generated ω-ADAs (up to 46 mM), α,ω-diols (up to 29 mM), ω-amino alcohols (up to 29 mM) and α,ω-diamines (up to 21 mM) from 100 mM corresponding FAME substrates with varying carbon chain length (C8, C10, and C12). Finally 12-ADA and 1,12-diol were purified with isolated yields of 66.5% and 52.5%, respectively. The multi-enzymatic cascade reactions reported herein present an elegant ‘greener’ alternative for the biosynthesis of various biopolymer monomers from renewable saturated fatty acids.
Imprinted Apportionment of Functional Groups in Multivariate Metal-Organic Frameworks
Feng, Liang,Wang, Kun-Yu,Lv, Xiu-Liang,Powell, Joshua A.,Yan, Tian-Hao,Willman, Jeremy,Zhou, Hong-Cai
supporting information, p. 14524 - 14529 (2019/10/02)
Sophisticated chemical processes widely observed in biological cells require precise apportionment regulation of building units, which inspires researchers to develop tailorable architectures with controllable heterogeneity for replication, recognition and information storage. However, it remains a substantial challenge to endow multivariate materials with internal sequences and controllable apportionments. Herein, we introduce a novel strategy to manipulate the apportionment of functional groups in multivariate metal-organic frameworks (MTV-MOFs) by preincorporating interlocked linkers into framework materials. As a proof of concept, the imprinted apportionment of functional groups within ZIF-8 was achieved by exchanging imine-based linker templates with original linkers initially. The removal of linker fragments by hydrolysis can be achieved via postsynthetic labilization, leading to the formation of architectures with controlled heterogeneity. The distributions of functional groups in the resulting imprinted MOFs can be tuned by judicious control of the interlocked chain length, which was further analyzed by computational methods. This work provides synthetic tools for precise control of pore environment and functionality sequences inside multicomponent materials.
Parallel anti-sense two-step cascade for alcohol amination leading to ω-amino fatty acids and α,ω-diamines
Sung, Sihyong,Jeon, Hyunwoo,Sarak, Sharad,Ahsan, Md Murshidul,Patil, Mahesh D.,Kroutil, Wolfgang,Kim, Byung-Gee,Yun, Hyungdon
supporting information, p. 4591 - 4595 (2018/10/23)
Running two two-step cascades in parallel anti-sense to transform an alcohol to an amine allowed the conversion of ω-hydroxy fatty acids (ω-HFAs) and α,ω-diols to the corresponding ω-amino fatty acids (ω-AmFAs) and α,ω-diamines, respectively. The network required only two enzymes namely an aldehyde reductase (AHR) and a transaminase (TA). Benzylamine served on the one hand as amine donor and on the other hand after deamination to benzaldehyde also as oxidant. All ω-HFAs tested were efficiently transformed to their corresponding ω-AmFAs using purified enzymes as well as a whole-cell system, separately expressing both the enzymes, with conversions ranging from 80-95%. Additionally, a single-cell co-expressing all enzymes successfully produced the ω-AmFAs as well as the α,ω-diamines with >90% yield. This system was extended by employing a lactonase, enabling the transformation of ?-caprolactone to its corresponding ω-AmFA with >80% conversion.
