Role of reinforcement types and silica nanoparticles on tribofilm growth at PTFE-Steel interface

2020 ◽  
Vol 143 ◽  
pp. 106035 ◽  
Author(s):  
Xuefeng Fan ◽  
Guitao Li ◽  
Yuexia Guo ◽  
Ligang Zhang ◽  
Yongkun Xu ◽  
...  
Keyword(s):  
2014 ◽  
Vol 34 (2) ◽  
pp. 255-265 ◽  
Author(s):  
Abderrahim Nemmar ◽  
Sumay Beegam ◽  
Priya Yuvaraju ◽  
Javed Yasin ◽  
Allen Shahin ◽  
...  

2013 ◽  
Vol 42 (31) ◽  
pp. 11271 ◽  
Author(s):  
Jakelyne Viana Coelho ◽  
Marina Silva Guedes ◽  
Deicy Barrera ◽  
Karim Sapag ◽  
Márcio César Pereira ◽  
...  

Author(s):  
Prasad Rama ◽  
Zareen Abbas

The role of nanoparticle shape in the interaction and adsorption of organic molecules on the particle surface is an unexplored area. On the other hand, such knowledge is not only...


Nanomaterials ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1799
Author(s):  
Aniello Costantini ◽  
Virginia Venezia ◽  
Giulio Pota ◽  
Aurelio Bifulco ◽  
Valeria Califano ◽  
...  

Mesoporous silica materials offer a unique opportunity for enzyme immobilization thanks to their properties, such as tuneable pore size, large surface area and easy functionalization. However, a significant enhancement of cellulase enzyme activity entrapped inside the silica pores still represents a challenge. In this work, we immobilized cellulase by adsorption on wrinkled silica nanoparticles (WSNs), obtaining an active and stable biocatalyst. We used pentanol as co-solvent to synthesize WSNs with enhanced inter-wrinkle distance in order to improve cellulase hosting. The physical-chemical and morphological characterization of WSNs and cellulase/WSNs was performed by thermogravimetric (TG), Fourier transform infrared (FT-IR), and transmission electron microscopy (TEM) analyses. The obtained results showed that this matrix generates a favourable microenvironment for hosting cellulase. The results of the catalytic assays and operational stability confirmed the key role of size, morphology and distribution of the pores in the successful outcome of the cellulase immobilization process. The immobilization procedure used allowed preserving most of the secondary structure of the enzyme and, consequently, its catalytic activity. Moreover, the same value of glucose yield was observed for five consecutive runs, showing a high operational stability of the biocatalyst.


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