When natural or live enzymes are utilised to initiate or speed up a chemical reaction, this process is referred to as enzyme biocatalysis. In 1858, Louis Pasteur conducted one of the earliest instances of contemporary enzyme biocatalysis. In order to create tartaric acid, Pasteur utilised a variety of microorganisms, including the mould Penicillium glaucum, as enzymes in a fermentation process. There are several applications for tartaric acid, including cleaning different metals, tanning leather, and food preservation. One of the first recorded cases of enzyme biocatalysis was carried out by renowned scientist Louis Pasteur. Metals have been used as catalysts in several sectors for many years. They may be made at a low cost and decompose naturally. They frequently perform quicker reactions at lower concentrations, which is one advantage of these enzymes employed in biocatalysis.
Frequently, they can operate in aqueous conditions and at less abrasive pH and temperature ranges.
They can be made in considerably greater quantities.
For a certain reaction, they may be made to be much more targeted.
Various plants (such as carrots and soy), fungi (such as mushrooms), bacteria, and animal organs like pigs' livers are just a few of the sources of these enzymes. Using recombinant DNA technology, newer versions of these enzymes can be created.
Stanislaw Dzwigaj
Sorbonne University, France
Thomas J Webster
Interstellar Therapeutics, United States
Dai Yeun Jeong
Asia Climate Change Education Center, Korea, Republic of
Vladislav Sadykov
Boreskov Institute of Catalysis, Russian Federation
Beatrice Vincenti
Sapienza University of Rome, Italy
Haibo Ge
Texas Tech University, United States
Pengju Wu
School of Energy and Power Engineering Jiangsu University, China
Yaxin Su
Donghua University, China
Isabel Oller Alberola
Plataforma Solar de Almería, Spain
Majed Alamoudi
King Abdulaziz University, Saudi ArabiaSubmit your abstract Today
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