2012
DOI: 10.1016/j.biortech.2012.04.015
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Effects of low intensity ultrasound on cellulase pretreatment

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Cited by 125 publications
(86 citation statements)
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“…The decreased proportion of a-helices and random segments and the increased proportion of b-sheets in hesperidinase were more conducive for isoquercitrin production. Wang et al reported similar results for changes in the composition of cellulase structure with an 8.85% decrease in a-helix content (Wang et al, 2012b). Combined with the results of the previous experiments, the small proportion of a-helices in the reaction system was more favorable for the reaction.…”
Section: Reusability and Stability Of Hesperidinase In A Segmented Flsupporting
confidence: 69%
“…The decreased proportion of a-helices and random segments and the increased proportion of b-sheets in hesperidinase were more conducive for isoquercitrin production. Wang et al reported similar results for changes in the composition of cellulase structure with an 8.85% decrease in a-helix content (Wang et al, 2012b). Combined with the results of the previous experiments, the small proportion of a-helices in the reaction system was more favorable for the reaction.…”
Section: Reusability and Stability Of Hesperidinase In A Segmented Flsupporting
confidence: 69%
“…Concurrent with these observations, the activity of the HRP enzyme showed 26% and 11% rise after ultrasound treatment at atmospheric and elevated static pressure, respectively. Similar results of structural transformations in the cellulase enzyme induced by ultrasound have been reported by Subhedar and Gogate (2014) and Wang et al (2012). Wang et al (2012) have reported a reduction of 8.85% in a-helix content with 29.5% increase in random coil content in the cellulase structure after sonication.…”
Section: Fluorescence Spectra and Circular Dichroism (Cd) Analysissupporting
confidence: 85%
“…The reduction in fluorescence intensity is an evidence of decrease of population of exposed tryptophan residues on HRP surface, probably due to aggregation of the protein after exposure. These conformational changes in enzyme essentially lead to exposure of hydrophobic amino acid groups and structures inside the enzyme molecules (Gulseren et al, 2007;Jambrak et al, 2008;Subhedar and Gogate, 2014;Wang et al, 2012), as further confirmed by the CD analysis described below. The conformational changes in protein structure of the enzyme have also been evaluated using CD spectra of native and ultrasound treated enzyme.…”
Section: Fluorescence Spectra and Circular Dichroism (Cd) Analysismentioning
confidence: 51%
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