Au nanoparticles (AuNPs) have shown the potential for a variety of applications due to their unique physical and chemical properties. In this study, a facile and affordable method for the synthesis of AuNPs via the liquefied mash of cassava starch has been described and the functionalized AuNPs by L-cysteine improved activity of recombinant xylanase was demonstrated. UV-Vis absorption spectroscopy, transmission electron microscopy, and zeta potential measurements were performed to characterize the AuNPs and monitor their synthesis. The presence of Au was confirmed by energy-dispersive X-ray spectroscopy (EDX) and the X-ray diffraction patterns showed that Au nanocrystals were face-centered cubic. The C=O stretching vibration in the Fourier transform infrared spectrum of AuNPs suggested that the hemiacetal C-OH of sugar molecules performed the reduction of Au³⁺ to Au⁰. The presence of C and O in the EDX spectrum and the negative zeta potential of AuNPs suggested that the biomolecules present in liquefied cassava mash were responsible for the stabilization of AuNPs. The surface of AuNPs was easily functionalized by L-cysteine, which improved the stability of AuNPs. Moreover, cysteine-functionalized AuNPs could significantly improve recombinant xylanase efficiency and stability.
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http://dx.doi.org/10.1007/s00449-016-1558-0 | DOI Listing |
The food enzyme endo-1,4-β-xylanase (4-β-d-xylan xylanohydrolase, EC 3.2.1.
View Article and Find Full Text PDFBiotechnol Lett
December 2024
Department of Life Sciences, Graduate School of Bioresources, Mie University, 1577 Kurimamachiya, Tsu, Mie, 514-8507, Japan.
The cell walls of red and green algae contain β-1,3-xylan, which is hydrolysed by the endo-type enzyme β-1,3-xylanase. Notably, only marine-bacteria-derived β-1,3-xylanases have been functionally characterised to date. In this study, we characterised the enzymatic properties of a potential β-1,3-xylanase (BcXyn26B) derived from the human gut bacterium, Bacteroides cellulosilyticus WH2.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Institute of Chemistry and Center for Computing in Engineering and Sciences, University of Campinas (UNICAMP), Campinas 13084-862, SP, Brazil.
GH10 xylanases and GH62 Arabinofuranosidases play key roles in the breakdown of arabinoxylans and are important tools in various industrial and biotechnological processes, such as renewable biofuel production, the paper industry, and the production of short-chain xylooligosaccharides (XOS) from plant biomass. However, the use of these enzymes in industrial settings is often limited due to their relatively low thermostability and reduced catalytic efficiency. To overcome these limitations, strategies based on enzymatic chimera construction and the use of metal ions and other cofactors have been proposed to produce new recombinant enzymes with improved catalytic activity and thermostability.
View Article and Find Full Text PDFbioRxiv
October 2024
Department of Molecular Biology, School of Biological Sciences, University of California San Diego, La Jolla, CA, United States of America.
, a genetically close relative of the model green alga , shows significant potential as a host for recombinant protein expression. Because of the close genetic relationship between and , this species offers an additional reference point for advancing our understanding of photosynthetic organisms, and also provides a potential new candidate for biotechnological applications. This study investigates C.
View Article and Find Full Text PDFInt J Biol Macromol
November 2024
Academy of National Food and Strategic Reserves Administration, No 11 Baiwanzhuang Avenue, Xicheng District, Beijing 100037, PR China. Electronic address:
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