Biocatalytic approach for the synthesis of chiral alcohols for the development of pharmaceutical intermediates and other industrial applications: A review DOI
Mohd. Javed Naim, Mohd Fazli Mohammat,

Putri Nur Arina Mohd Ariff

et al.

Enzyme and Microbial Technology, Journal Year: 2024, Volume and Issue: 180, P. 110483 - 110483

Published: July 17, 2024

Language: Английский

The E factor at 30: a passion for pollution prevention DOI Creative Commons
Roger A. Sheldon

Green Chemistry, Journal Year: 2023, Volume and Issue: 25(5), P. 1704 - 1728

Published: Jan. 1, 2023

Publication of the E Factor drew attention to problem waste in chemicals manufacture. Thirty yeas later it is abundantly clear that underlying cause global environmental problems, from climate change plastic pollution.

Language: Английский

Citations

150

Biocatalysis as Key to Sustainable Industrial Chemistry DOI
Andrés R. Alcántara, Pablo Domı́nguez de Marı́a, Jennifer A. Littlechild

et al.

ChemSusChem, Journal Year: 2022, Volume and Issue: 15(9)

Published: March 3, 2022

The role and power of biocatalysis in sustainable chemistry has been continuously brought forward step by to its present outstanding position. problem-solving capabilities have realized numerous substantial achievements biology, engineering. Advances breakthroughs the life sciences interdisciplinary cooperation with clearly accelerated implementation biocatalytic synthesis modern chemistry. Resource-efficient manufacturing processes already provided benefits as well customer-centric value creation pharmaceutical, food, flavor, fragrance, vitamin, agrochemical, polymer, specialty, fine chemical industries. Biocatalysis can make significant contributions not only processes, but also design completely new value-creation chains. now be considered a key enabling technology implement

Language: Английский

Citations

102

Lipase immobilization via cross-linked enzyme aggregates: Problems and prospects – A review DOI Creative Commons
C. S. T. de Sampaio, Joelise Alencar Figueira ANGELOTTI, Roberto Fernandéz‐Lafuente

et al.

International Journal of Biological Macromolecules, Journal Year: 2022, Volume and Issue: 215, P. 434 - 449

Published: June 22, 2022

In this review we have focused on the preparation of cross-linked enzyme aggregates (CLEAs) from lipases, as these are among most used in bioprocesses. This immobilization method is considered very attractive due to simplicity, non-use supports and possibility using crude extracts. CLEAs provide lipase stabilization under extreme temperature or pH conditions presence organic solvents, addition preventing leaching aqueous medium. However, it presents some problems limitations their use. The refer mainly crosslinking step, may be solved an aminated feeder. handling been tackled designing magnetic-CLEAs trapping particles with better mechanical properties, substrate diffusion has reduced by producing more porous-CLEAs, etc. co-immobilization combi-CLEAs also a new tendency. Therefore, explores methodology aimed at its applications.

Language: Английский

Citations

88

Decarbonizing the chemical industry: A systematic review of sociotechnical systems, technological innovations, and policy options DOI

Changwoo Chung,

Jinsoo Kim, Benjamin K. Sovacool

et al.

Energy Research & Social Science, Journal Year: 2023, Volume and Issue: 96, P. 102955 - 102955

Published: Jan. 23, 2023

Language: Английский

Citations

63

Marine plastics, circular economy, and artificial intelligence: A comprehensive review of challenges, solutions, and policies DOI
Seyed reza seyyedi, Elaheh Kowsari, Seeram Ramakrishna

et al.

Journal of Environmental Management, Journal Year: 2023, Volume and Issue: 345, P. 118591 - 118591

Published: July 7, 2023

Language: Английский

Citations

54

Supramolecular complex catalyzed green synthesis of 9-(2-Ethylhexyl) carbazole: Structural, optical and DFT investigations DOI
Priyanka Behera,

T. Jaison Jose,

D. S. Ramakrishna

et al.

Journal of Molecular Structure, Journal Year: 2024, Volume and Issue: 1308, P. 138089 - 138089

Published: March 19, 2024

Language: Английский

Citations

22

The role of binding modules in enzymatic poly(ethylene terephthalate) hydrolysis at high-solids loadings DOI Creative Commons
Rosie Graham, Erika Erickson, Richard K. Brizendine

et al.

Chem Catalysis, Journal Year: 2022, Volume and Issue: 2(10), P. 2644 - 2657

Published: Aug. 23, 2022

In nature, enzymes that deconstruct biological polymers, such as cellulose and chitin, often exhibit multi-domain architectures, comprising a catalytic domain non-catalytic binding module; the latter serves to increase enzyme concentration at substrate surface. This architecture has been shown improve hydrolysis of poly(ethylene terephthalate) (PET) using engineered cutinase enzymes. Here, we examine role accessory modules industrially relevant PET solids loadings necessary for cost-effective enzymatic recycling. Using thermostable variant leaf compost (LCC), produced synthetic fusion constructs LCC with five type A carbohydrate-binding (CBMs). At below 10 wt %, CBMs aromatic monomer yield from PET, but above this threshold, conversion extents up 97% are reached no added benefits presence CBM fusions. suggests herein studied not industrial

Language: Английский

Citations

42

On optimization of enzymatic processes: Temperature effects on activity and long-term deactivation kinetics DOI Creative Commons

Md Fauzul Kabir,

Lu‐Kwang Ju

Process Biochemistry, Journal Year: 2023, Volume and Issue: 130, P. 734 - 746

Published: May 30, 2023

Enzymatic processes are industrially important. Process duration, temperature, and pH critical factors to optimize. Longer can improve economics by requiring less enzyme. Both temperature affect enzymes, but has far stronger interactive effects with process which scarcely been considered. To fill this technology gap, we investigated both short- long-term on Aspergillus niger carbohydrases. For short-term effects, enzyme activities were measured at different temperatures regressed a model that considered catalytic activation-energy protein-folding. The model-determined optima were: α-galactosidase, 57.6 °C; sucrase, 53.4 pectinase, 49.4 xylanase, 50.4 cellulase, 46.5 °C. Long-term evaluated 40, 52, 55, 60, 65 °C for 72 h determine the activity decay constants activation energies. observed order of stability was sucrase > α-galactosidase pectinase while cellulase showed more complex kinetics. These models enabled prediction cumulative enzymatic performance durations. verified experimental results soybean molasses hydrolysis, giving 51% higher stachyose conversion after 54 (predicted optimum) than 60 developed approach taken valuable optimizing processes, sustainability environmental friendliness.

Language: Английский

Citations

38

Engineering ketoreductases for the enantioselective synthesis of chiral alcohols DOI Creative Commons
Qiao Li,

Zhiyuan Luo,

Haomin Chen

et al.

Chemical Communications, Journal Year: 2023, Volume and Issue: 59(49), P. 7518 - 7533

Published: Jan. 1, 2023

This review summarises the use of engineered ketoreductases (KREDS), both as whole microbial cells and isolated enzymes, in highly enantiospecific reduction prochiral ketones.

Language: Английский

Citations

30

From green to circular chemistry paved by biocatalysis DOI Creative Commons
Pedro Lozano, Eduardo Garcı́a-Verdugo

Green Chemistry, Journal Year: 2023, Volume and Issue: 25(18), P. 7041 - 7057

Published: Jan. 1, 2023

Biocatalysts raised by the green chemistry and circular principles can constitute most important efficient strategy for achieving many of 17 Sustainable Development Goals launched UN.

Language: Английский

Citations

29