2005
DOI: 10.1016/j.ijbiomac.2005.07.002
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The contribution of ionic interactions to the conformational stability and function of polygalacturonase from A. niger

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Cited by 13 publications
(4 citation statements)
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“…However, in these conditions the enzymes retained a residual activity of 50% and 97%, respectively. These results are in agreement with the effect described by Jyothi et al (2005). At high pH values, alterations can be produced in secondary and tertiary protein structures.…”
Section: Exo-pg and Xylanase Stabilitysupporting
confidence: 92%
“…However, in these conditions the enzymes retained a residual activity of 50% and 97%, respectively. These results are in agreement with the effect described by Jyothi et al (2005). At high pH values, alterations can be produced in secondary and tertiary protein structures.…”
Section: Exo-pg and Xylanase Stabilitysupporting
confidence: 92%
“…The decrease in fluorescence with the progress of the PL treatment is consistent with the progressive unfolding of the enzyme, which exposes tryptophan residues to a hydrophilic environment where their quantum yield is lower. A similar result has been found for the inactivation of PG by ultrasound (Ma et al, 2015) and by changing the pH from its optimum pH (4.3) to 7.0 (Jyothi, Singh, & Appu Rao, 2005). A reduction of fluorescence intensity upon PL treatment has also been reported for β-lactoglobulin, sodium caseinate, α-lactalbumin (Elmnasser et al, 2008), and PPO (Pellicer et al, 2018).…”
Section: Steady-state Tryptophan Fluorescencesupporting
confidence: 72%
“…A broad pI kit (3.5-9.3) was used as standard. Protein (3 mg/mL) and markers were loaded directly onto the gel with sample application pieces (16).…”
Section: Introductionmentioning
confidence: 99%