Thermochemical, volumetric and spectroscopic properties of lysozyme–poly(ethylene) glycol system

Zielenkiewicz, W.; Świerzewski, Rafał; Attanasio, Francesco; Rialdi, G.

doi:10.1007/s10973-005-7417-x

Cited by 32 publications

(18 citation statements)

References 29 publications

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“…PEG binds an intermediate in the folding pathway of carbonic anhydrase, therefore prevents self-association and promotes correct refolding [43][44][45]. PEG interacts with the hydrophobic side chains exposed upon unfolding at high temperatures [46]. PEG has been successfully used for refolding of interferon [47], xylanase [48], and insulin-like growth factor (IGF-1) [49] from inclusion bodies.…”

Section: Polyethylene Glycol (Peg)mentioning

confidence: 99%

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Alibolandi¹,

Mirzahosei²

2011

American J. of Biochemistry and Molecular Biology

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Escherichia coli is one of the most widely used hosts for the production of recombinant proteins but insoluble expression of heterologous proteins is a major bottleneck in production of recombinant proteins in E. coli. In vitro refolding of inclusion body into proteins with native conformations is a solution for this problem but there is a need for optimization of condition for each protein specifically. Several approaches have been described for in vitro refolding; most of them involve the use of additives for assisting correct folding. Cosolutes play a major role in refolding process and can be classified according to their function as aggregation suppressors and folding enhancers. This paper presents a review of additives that are used in refolding process of insoluble recombinant proteins in small scale and industrial processes.

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Section: Polyethylene Glycol (Peg)mentioning

confidence: 99%

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Alibolandi¹,

Mirzahosei²

2011

American J. of Biochemistry and Molecular Biology

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“…One of the applications of PEG is as a macromolecular crowding agent. 8 The term ''thermal stability'' or ''thermostability'' refers to protein resistance to adverse intrinsic and extrinsic environmental influences, that is, the inherent properties of a protein to resist unfolding and inactivation under exposure to high temperatures or other deleterious agents. 9 Studies related to the stability of lysozyme in the presence of PEG had been made.…”

Section: Introductionmentioning

confidence: 99%

“…9 Studies related to the stability of lysozyme in the presence of PEG had been made. In the study by Zielenkiewicz et al, 8 the addition of PEG to the buffered lysozyme solution changed the thermal stability of lysozyme; lowering the unfolding temperature with the increase of PEG concentration. The study by Hancock and Hsu 10 showed that lysozyme unfolded at lower temperatures in 20% (w/w) PEG 1000, and native lysozyme conformation was minimally affected by the presence of 5 to 10% (w/w) PEG 300.…”

Section: Introductionmentioning

confidence: 99%

“…10,12 In spite of PEG ability to lower the solvent polarity, so as to stabilize the unfolded state, it is also expected that PEG would favor the compact, native state of protein due to a larger excluded volume of its unfolded state. 8 Low-molar weight PEGs are excluded from the protein surface, stabilizing its native conformation by a phenomenon of hydration, while high-molar weight PEGs interact with many hydrophobic sites of proteins, thus stabilizing their unfolded conformation (inactive). 13 Considering the high potential of GFP as a bioindicator, and PEG as a protein stabilizer, we studied the thermal stability of GFP in the presence of different PEG molar weights.…”

Section: Introductionmentioning

confidence: 99%

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Effect of polyethylene glycol on the thermal stability of green fluorescent protein

Novaes

Mazzola

Pessoa

et al. 2009

Biotechnology Progress

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Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. Some polymers, such as polyethylene glycol, are often used as modifiers of characteristics of biological macromolecules, to improve the biochemical activity and stability of proteins or drug bioavailability. The aim of this study was to evaluate the thermal stability of GFP in the presence of different PEG molar weights at several concentrations and exposed to constant temperatures, in a range of 70-95 degrees C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were almost constant for temperatures of 85, 90, and 95 degrees C, despite the PEG concentration or molar weight studied. Even though PEG can stabilize proteins, only at 75 degrees C, PEG 600 and 4,000 g/mol stabilized GFP.

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“…Some polymers are often used as modifiers of biological macromolecules to improve the biochemical activity of proteins or drug bioavailability (Zielenkiewicz et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

The influence of pH, polyethylene glycol and polyacrylic acid on the stability of stem bromelain

Novaes

Jozala

Mazzola

et al. 2014

Braz. J. Pharm. Sci.

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Enzyme stability is critical in biotechnology, pharmaceutical and cosmetic industries. Investigations on this subject have drawn attention because of its practical application. Bromelain is a thiol-endopeptidase, obtained from pineapple (Ananas comosus), known for its clinical and therapeutic applications, particularly to selective burn debridement and improvement of antibiotic action and anti-inflammatory activities. To date, the use of bromelain in pharmacological or industrial applications is limited, due to commercial availability, costs, and sensitivity to pH and temperature. Therefore, a better understanding of enzyme stability would be of great interest. The aim of this study was to evaluate bromelain activity and stability in several pH (2.0 to 8.0) and in polyethylene glycol and polyacrylic acid solutions. We observed that bromelain was able to maintain its stability at pH 5.0 for the temperatures studied. PEG solutions increased bromelain stability, but PAA solutions had the opposite effect.Uniterms: Bromelain/pH stability. Polyethylene glycol/enzyme stability. Polyacrylic acid/enzyme stability. Enzyme/stability.Estabilidade de enzimas é uma questão fundamental em indústrias biotecnológicas, farmacêuticas e cosméticas. As investigações sobre o assunto têm chamado a atenção por sua aplicação prática. A bromelina é uma tiol-endopeptidase, obtida a partir do abacaxi (Ananas comosus). É conhecida por suas aplicações clínicas e terapêuticas, especialmente para desbridamento seletivo de queimaduras, melhoria de ações antibiótica e de atividades anti-inflamatórias. Até o momento, a utilização da bromelina em aplicações farmacológicas industriais é limitada, devido à disponibilidade comercial, os custos, a sensibilidade ao pH e temperatura. Portanto, a maior compreensão da estabilidade desta enzima seria de grande interesse. O objetivo deste estudo foi avaliar a estabilidade da atividade da bromelina em vários pH (2,0 a 8,0) e em soluções de polietilenoglicol e de ácido poliacrílico. Observamos que a bromelina foi capaz de manter a sua estabilidade em pH 5.0, em todas as temperaturas estudadas. Soluções de PEG aumentaram a estabilidade da bromelina, enquanto que soluções de PAA obtiveram efeito oposto.Unitermos: Bromelina/estabilidade em pH. Polietilenoglicol/estabilidade de enzimas. Ácido poliacrílico/ estabilidade de enzimas. Enzimas/estabilidade.

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Thermochemical, volumetric and spectroscopic properties of lysozyme–poly(ethylene) glycol system

Cited by 32 publications

References 29 publications

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Effect of polyethylene glycol on the thermal stability of green fluorescent protein

The influence of pH, polyethylene glycol and polyacrylic acid on the stability of stem bromelain

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