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Fatigue crack propagation was modeled by using the cyclic plasticity material properties and fatigue constants for crack initiation. The cyclic elastic-plastic stress-strain field near the crack tip was analyzed using the finite element method with the implementation of a robust cyclic plasticity theory. An incremental multiaxial fatigue criterion was employed to determine the fatigue damage. A straightforward method was developed to determine the fatigue crack growth rate. Crack propagation behavior of a material was obtained without any additional assumptions or fitting. Benchmark Mode I fatigue crack growth experiments were conducted using 1070 steel at room temperature. The approach developed was able to quantitatively capture all the important fatigue crack propagation behaviors including the overload and the R-ratio effects on crack propagation and threshold. The models provide a new perspective for the R-ratio effects. The results support the notion that the fatigue crack initiation and propagation behaviors are governed by the same fatigue damage mechanisms. Crack growth can be treated as a process of continuous crack nucleation.

BackgroundBiocatalytic processes often require a full recycling of biocatalysts to optimize economic benefits and minimize waste disposal. Immobilization of biocatalysts onto particulate carriers has been widely explored as an option to meet these requirements. However, surface properties often affect the amount of biocatalysts immobilized, their bioactivity and stability, hampering their wide applications. The aim of this work is to explore how immobilization of lipases onto magnetite nanoparticles affects their biocatalytic performance under carefully controlled surface modification.Methodology/Principal FindingsMagnetite nanoparticles, prepared through a co-precipitation method, were coated with alkyl silanes of different alkyl chain lengths to modulate their surface hydrophobicity. Candida rugosa lipase was then directly immobilized onto the modified nanoparticles through hydrophobic interaction. Enzyme activity was assessed by catalytic hydrolysis of p-nitrophenyl acetate. The activity of immobilized lipases was found to increase with increasing chain length of the alkyl silane. Furthermore, the catalytic activities of lipases immobilized on trimethoxyl octadecyl silane (C18) modified Fe3O4 were a factor of 2 or more than the values reported from other surface immobilized systems. After 7 recycles, the activities of the lipases immobilized on C18 modified nanoparticles retained 65%, indicating significant enhancement of stability as well through hydrophobic interaction. Lipase immobilized magnetic nanoparticles facilitated easy separation and recycling with high activity retaining.Conclusions/SignificanceThe activity of immobilized lipases increased with increasing alkyl chain length of the alkyl trimethoxy silanes used in the surface modification of magnetite nanoparticles. Lipase stability was also improved through hydrophobic interaction. Alkyl silane modified magnetite nanoparticles are thus highly attractive carriers for enzyme immobilization enabling efficient enzyme recovery and recycling.

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