2016
DOI: 10.1016/j.procbio.2016.05.005
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Unanticipated behaviour of sorbitol towards the stability and activity of stem bromelain: An outlook through biophysical techniques

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Cited by 21 publications
(14 citation statements)
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“…Thus, adding sorbitol may have universal applicability for improving the thermostability of enzymes. It has been proved that sorbitol can improve the thermostability of xylanase (Kumar et al, 2017), trypsin (Mohammad Pazhang et al, 2015) and bromelain (Rani & Pannuru, 2016). Our results…”
Section: Discussionsupporting
confidence: 68%
See 1 more Smart Citation
“…Thus, adding sorbitol may have universal applicability for improving the thermostability of enzymes. It has been proved that sorbitol can improve the thermostability of xylanase (Kumar et al, 2017), trypsin (Mohammad Pazhang et al, 2015) and bromelain (Rani & Pannuru, 2016). Our results…”
Section: Discussionsupporting
confidence: 68%
“…The hydration layer makes the structure of water molecules more orderly and enhances the hydrophobic interaction between non-polar groups, which reduces the direct interaction between water and enzyme molecules. At the same time, the hydrogen bonds between sorbitol and tryptophan make hydrophobic amino acids curl inward to stabilize the conformation of enzymes (Ajito et al, 2018;Kumar et al, 2017;Rani & Pannuru, 2016). Thus, adding sorbitol may have universal applicability for improving the thermostability of enzymes.…”
Section: Discussionmentioning
confidence: 99%
“…Quercetin, composed of five hydroxyls, is grouped among the most efficient antioxidant flavonoid . Its high antioxidant activity is attributed to its ability to prevent radical processes in cells through three mechanisms: (i) sequestration action of O 2 , (ii) reaction with peroxyl radicals, inhibiting lipid peroxidation, and (iii) iron chelating action decreasing OH‐ formation . Then, quercetin is usually used as positive control in in vitro antioxidant activity tests.…”
Section: Resultsmentioning
confidence: 99%
“…In the hydrophobic core of a folded protein Trp has high fluorescence intensity. In an unfolded protein, Trp is exposed to a polar environment and this results in a decrease in fluorescence (Rani and Pannuru, 2016; Rani and Venkatesu, 2015; Rani and Venkatesu, 2016). The combination of 1 H NMR data and Figure S5 suggested that bromelain and the surfactant together formed a more compact structure via hydrophobic interaction.…”
Section: Discussionmentioning
confidence: 99%
“…Studies on enhancing enzyme activity and stability have always been of great importance for both basic research and industrial applications (Arshad et al, 2014; Manzoor et al, 2016; Rani and Pannuru, 2016; Rani and Venkatesu, 2015; Rani and Venkatesu, 2016; Rathnavelu et al, 2016; Xue et al, 2019). The conformational stability of bromelain increases with increasing polyol size and the proteolytic activity of bromelain changes in the opposite order; among xylitol, erythritol, ethylene glycol, glycerol, and sorbitol, sorbitol is the weakest stabilizer for bromelain whereas it increases the activity of bromelain the most (Rani and Pannuru, 2016; Rani and Venkatesu, 2015). GdnHCl and trehalose have opposite effects on bromelain activity; the former denatures bromelain while the latter stabilizes bromelain.…”
Section: Introductionmentioning
confidence: 99%