cis-Prenyltransferase catalyzes the synthesis of Z,E-mixed prenyl diphosphates by a condensation of isopentenyl diphosphate to an allylic diphosphate. A novel gene encoding a cis-prenyltransferase is cloned from Thermobifida fusca. It showed a unique substrate specificity accepting dimethylallyl diphosphate as a shortest allylic substrate, and synthesizes polyprenyl products up to C(70).
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http://dx.doi.org/10.1016/j.jbiosc.2009.02.006 | DOI Listing |
J Hazard Mater
January 2025
Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio Av. 7, Vilnius 10257, Lithuania.
Enzymatic degradation of plastic pollution offers a promising environmentally friendly waste management strategy, however, suitable biocatalysts must be screened and developed. Traditional screening methods using soluble or solubilised polymers do not necessarily identify enzymes that are effective against solid or crystalline polymers. This study presents a simple, time-saving and cost-effective method for identifying microorganisms and enzymes capable of degrading polymeric films.
View Article and Find Full Text PDFBMC Biotechnol
December 2024
Environmental Microbiology and Biotechnology Unit, Department of Microbiology, Faculty of Biological Sciences, University of Calabar, Calabar, Nigeria.
Background: The eco-friendly transformation of agro-industrial wastes through microbial bioconversion could address sustainability challenges in line with the United Nations' Sustainable Development Goals. The bulk of agro-industrial waste consists of lignocellulosic materials with fermentable sugars, predominantly cellulose and hemicellulose. A number of pretreatment options have been employed for material saccharification toward successful fermentation into second-generation bioethanol.
View Article and Find Full Text PDFEnzyme Microb Technol
December 2024
School of Biotechnology and Key Laboratory of Industrial Biotechnology Ministry of Education, China; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi 214122 China. Electronic address:
The substantial accumulation of polyethylene terephthalate (PET) plastic waste in the environment has exacerbated the issue of plastic pollution. The biodegradation of PET plastics using biological enzymes has garnered considerable attention due to its efficiency and environmentally friendly nature. Nevertheless, the low binding affinity of PET plastics presents a significant limitation to the application of biocatalysts in their degradation.
View Article and Find Full Text PDFBiotechnol Biofuels Bioprod
December 2024
Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN, 37235, USA.
Background: Cellulose, an abundant biopolymer, has great potential to be utilized as a renewable fuel feedstock through its enzymatic degradation into soluble sugars followed by sugar fermentation into liquid biofuels. However, crystalline cellulose is highly resistant to hydrolysis, thus industrial-scale production of cellulosic biofuels has been cost-prohibitive to date. Mechanistic studies of enzymes that break down cellulose, called cellulases, are necessary to improve and adapt such biocatalysts for implementation in biofuel production processes.
View Article and Find Full Text PDFBioresour Technol
November 2024
School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China; State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China. Electronic address:
Biodegradation, particularly via enzymatic degradation, has emerged as an efficient and eco-friendly solution for Poly (ethylene terephthalate) (PET) pollution. The production of PET hydrolases plays a role in the large-scale enzymatic degradation. However, an effective variant, 4Mz, derived from Thermobifida fusca cutinase (Tfu_0883), was previously associated with a significant reduction in yield when compared to the wild-type enzyme.
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