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http://dx.doi.org/10.3760/cma.j.cn112151-20240418-00257 | DOI Listing |
Bioresour Technol
February 2025
Department of Microbiology, Central University of Haryana, Mahendergarh, Haryana 123029, India. Electronic address:
The laccase from the newly isolated Trametes cubensis was investigated for its potential to degrade malachite green (MG) dye. Optimized solid-substrate fermentation enhanced laccase production by 8.8-fold, reaching an activity of 6577.
View Article and Find Full Text PDFBiosens Bioelectron
January 2025
College of Food and Biological Engineering, Jimei University, Xiamen 361021, PR China. Electronic address:
The primary challenge hindering the broad application of surface-enhanced Raman scattering (SERS) is the variability in substrate performance due to site differences, leading to unstable detection results. Thus, the current work reports the constant potential deposition of gold (Au) nanostructure on a hybrid nanoporous gold (npAu)-Au mirror template to generate highly stable monolithic Au-saturated npAu@Au-mirror substrate. By systematically adjusting electrochemical variables, different sizes, shapes, and nanogaps of Au nanostructure are generated with high-intensity electromagnetic field regions (hot junctions) for enhanced SERS response.
View Article and Find Full Text PDFAnal Chem
November 2024
College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000, China.
Conventional solid-based SERS substrates often face challenges with inconsistent sample distribution, while liquid-based SERS substrates are prone to aggregation and precipitation, resulting in irreproducible signals in both cases. In this study, we tackled this dilemma by designing and synthesizing raspberry-like plasmonic nanoaggregates that exhibit a high density of hotspots and are colloidally stable at the same time. In particular, the nanoaggregates consist of a core made of functionalized polystyrene (PS) microspheres, which act as a template for rapid self-assembly of Au@Ag core-shell nanoparticles to form raspberry-like hierarchical nanoaggregates within 5 min of mixing.
View Article and Find Full Text PDFZhonghua Bing Li Xue Za Zhi
October 2024
Department of Pathology, the Affiliated Drum Tower Hospital of Nanjing University Medical School, Nanjing 210008, China.
World J Microbiol Biotechnol
August 2024
Jiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Dye-decolorizing peroxidases (DyPs) belong to a novel superfamily of heme peroxidases that can oxidize recalcitrant compounds. In the current study, the GlDyP2 gene from Ganoderma lucidum was heterologously expressed in Escherichia coli, and the enzymatic properties of the recombinant GlDyP2 protein were investigated. The GlDyP2 protein could oxidize not only the typical peroxidase substrate ABTS but also two lignin substrates, namely guaiacol and 2,6-dimethoxy phenol (DMP).
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