Mechanism of solvent induced thermal stabilization of papain

Sathish, Hasige A.; Kumar, Pradeep; Prakash, V.

doi:10.1016/j.ijbiomac.2007.05.009

Cited by 34 publications

(36 citation statements)

References 41 publications

(45 reference statements)

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“…In addition, the presence of an intermediate state formed during the protein denaturation process contributes to this fact [4,15].…”

Section: Discussionmentioning

confidence: 99%

“…It is composed of a single polypeptide chain of 212 amino acid residues folded into the L and R domain, forming a cavity where its active site is located. The histidine (His-159), aspartic acid (Asp-158) and cysteine (Cys-25) are the residues that compose its active site [2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

“…Several substances are able to affect the stability of the folded protein, maintaining the native structure, particularly sugars and polyols [4].…”

Section: Introductionmentioning

confidence: 99%

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Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

et al. 2007

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Papain is a proteolytic enzyme with restricted applications due to its limited stability. Cyclodextrins are widely used in pharmaceutical formulations once they are able to form complexes with other molecules, improving their stability and bioavailability. The purpose of the present paper was to analyze complexes formed by papain/hydroxypropyl-β-cyclodextrin and papain/β-cyclodextrin by thermal analysis and cytotoxicity tests to verify their possible interactions and toxicological behavior. Complex solutions were prepared at different molar ratios and collected as a function of time to be lyophilized and analyzed. Results showed changes in endothermic events and cytotoxicity profiles. A complex formation for both complexes is observed; nevertheless, β-cyclodextrin was able to change the enzyme characteristics more efficiently.

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“…In addition, the presence of an intermediate state formed during the protein denaturation process contributes to this fact [4,15].…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

et al. 2007

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“…The development of a broad range of techniques has led to the identification and characterization of stable folding intermediates, termed "molten globule", (MG) which have been shown to be compact structures with a pronounced secondary structure which lack rigid tertiary structures [7][8][9][10]. Recent evidence, however, supports the idea that the molten globules may also possess well-defined tertiary contacts [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic Study of Intermediate State of Papain Induced by n-Alkyl Sulfates at Two Different pH Values: A Spectroscopic Approach

Chamani¹,

Heshmati²,

Rajabi³

et al. 2009

TOSURSJ

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Abstract:The formation of the intermediate state of papain was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; and sodium dodecyl sulfate, SDS at different concentrations. A systematic investigation of n-alkyl sulfates induced conformational alteration in molten globule state under an acidic condition and the native state of papain was examined by tryptophan fluorescence, 1-anilino 8-naphtalene sulfonic acid (ANS) binding and UV absorbance. The addition of n-alkyl sulfates to molten globule state at pH 2 shows a decrease in tryptophan fluorescence intensity and quenched ANS fluorescence relative to the native state that leads to enhancement in tryptophan fluorescence and an increase in ANS fluorescence as well. In the presence of n-alkyl sulfates in various conditions, two intermediate (I A and I B ) with different conformations were obtained at acidic and native states, respectively. Thus, we can assume that the intermediate states in folding and unfolding pathways in various conditions have different structures. The results show that SDS is much more effective than SDeS and SOS for the formation of the intermediate states for papain in the two different pathways due to the presence of its hydrophobic tail. Therefore, hydrophobic interactions play an important role in inducing the two different intermediates along the two various thermodynamic pathways.

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“…16 The maximal activity of papain was reported by several independent groups to be at around 55 8C [17][18][19][20][21][22] while papain denatures at 83-84 8C. 22,23 The…”

mentioning

confidence: 99%

Lactose‐containing hydrogels for enzyme stabilization

Huang

Chai

Warmin

et al. 2016

J. Polym. Sci. Part A: Polym. Chem.

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A lactose-containing monomer, N-(2-lactosylethyl)acrylamide, was synthesized and polymerized with N-hydroxyethyl acrylamide and 1 wt % of N, N'-methylenebis(acrylamide) and potassium persulfate as the initiator to produce hydrogels. The weight percent of N-(2-lactosylethyl)acrylamide were increased from 0 to 100% in increments of 10%. Hydrogels were successfully produced with up to 90 wt % of N-(2-lactosylethyl)acrylamide. Gelation was confirmed by inverted vial tests and rheology measurements. The as-prepared hydrogels were used for papain stabilization against heat burden and papain that was loaded into hydrogels showed 45% more activity after heating as compared to papain that was heated without hydrogel stabilization. This hydrogel stabilization technique has potential applications in preserving enzyme activity.

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Mechanism of solvent induced thermal stabilization of papain

Cited by 34 publications

References 41 publications

Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

Thermodynamic Study of Intermediate State of Papain Induced by n-Alkyl Sulfates at Two Different pH Values: A Spectroscopic Approach

Lactose‐containing hydrogels for enzyme stabilization

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