Towards increasing chemical and thermal stability of lysozyme with a simulated honey sugar cocktail

Wong, Yin How; Lim, Chze Huey; Kadir, Habsah Abdul; Tayyab, Saad

doi:10.1039/c4ra09606a

Cited by 8 publications

(2 citation statements)

References 35 publications

(50 reference statements)

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“…Hence, the stabilization of proteins plays a key role in these applications. Earlier, osmolytes had been used as a protein stabilizer, but natural osmolytes like honey could only marginally stabilize lysozymes against chemical denaturation by GdnHCl . Metal nanoclusters thus could serve as an alternative for the structural stability of lysozymes and other similar amyloidogenic proteins.…”

Section: Resultsmentioning

confidence: 99%

Temperature-Induced Luminescence Intensity Fluctuation of Protein-Protected Copper Nanoclusters: Role of Scaffold Conformation vs Nonradiative Transition

Sebastian,

Aarya

et al. 2024

ACS Omega

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Protein-scaffolded atomically precise metal nanoclusters (NCs) have emerged as a promising class of biofriendly nanoprobes at the forefront of modern research, particularly in the area of sensing. The photoluminescence (PL) intensity of several nanoclusters showed a systematic temperature-dependent fluctuation, but the mechanism remains ambiguous and is poorly understood. We tried to shed some light on this mechanistic aspect by testing a couple of hypotheses: (i) conformational fluctuation of the protein scaffold-mediated PL intensity fluctuation and (ii) PL intensity fluctuation due to the variation in the radiative and nonradiative transition rates. Herein, the PL intensity of the lysozyme-capped copper nanocluster (Lys-Cu NC) showed excellent temperature dependency; upon increasing the temperature, the PL intensity gradually decreased. However, contrasting effects can be seen when the nanocluster is exposed to a chemical denaturant (guanidine hydrochloride (GdnHCl)); the PL intensity increased with the increase in the GdnHCl concentration due to the change in the ionic strength of the medium. This discrepancy clearly suggests that the thermal PL intensity fluctuation cannot be explained by a change in the scaffold conformation. Furthermore, upon closer investigation, we observed a 2-fold increase in the nonradiative decay rate of the Lys-Cu NC at the elevated temperature, which could reasonably explain the decrease in the PL intensity of the nanocluster at the higher temperature. Additionally, from the result, it was evident that the protein scaffold−metal core interaction played a key role here in stabilizing each other; hence, the scaffold structure remained unaffected even in the presence of chemical denaturants.

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Section: Resultsmentioning

confidence: 99%

Temperature-Induced Luminescence Intensity Fluctuation of Protein-Protected Copper Nanoclusters: Role of Scaffold Conformation vs Nonradiative Transition

Sebastian,

Aarya

et al. 2024

ACS Omega

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“…4, polysaccharide/Ly systems displayed different phase behaviors when suffered from heat-treatment (20-80°C) for 30 min and exhibited a temperaturedependent manner. Ly solutions were transparent at temperature under thermal denaturation temperature (70°C), showing a very good heat resistance (Wong et al 2014). However, denaturation, self-aggregation and phase separation occurred when temperature higher than 70°C.…”

Section: Activity Of Ly In the Absence And Presence Of Polysaccharidesmentioning

confidence: 99%

Effect of physical interactions on structure of lysozyme in presence of three kinds of polysaccharides

Jin

Wang

et al. 2018

J Food Sci Technol

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In this work the influences of -carrageenan (CRG), konjac glucomannan (KGM) and inulin on lysozyme (Ly)'s structure, activity, and their complex phase behavior were investigated through spectroscopy and activity measurement in heated and unheated conditions. It was found that the impact on the structure and activity of Ly was determined by the interactions with polysaccharides. After heat treatment, KGM and CRG improved the stability of complex systems. However, inulin did not have significant impact. Heating process promoted to change the structure of Ly, and the intervention retard following the sequence of CRG> KGM > inulin. The worthwhile work indicated protein's structure and activity could be regulated by the interaction with polysaccharide, which might provide theoretical basis for food preservation and processing in different temperature treatments. Besides, the bidirectional effects of polysaccharide on protein would be beneficial to rational selection of functional properties of polysaccharide/protein systems.

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Environment induced self-aggregation behavior of κ-carrageenan/lysozyme complex

Jin

Zhang

et al. 2015

Bioactive Carbohydrates and Dietary Fibre

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Towards increasing chemical and thermal stability of lysozyme with a simulated honey sugar cocktail

Cited by 8 publications

References 35 publications

Temperature-Induced Luminescence Intensity Fluctuation of Protein-Protected Copper Nanoclusters: Role of Scaffold Conformation vs Nonradiative Transition

Temperature-Induced Luminescence Intensity Fluctuation of Protein-Protected Copper Nanoclusters: Role of Scaffold Conformation vs Nonradiative Transition

Effect of physical interactions on structure of lysozyme in presence of three kinds of polysaccharides

Environment induced self-aggregation behavior of κ-carrageenan/lysozyme complex

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