Overview of the Stability of α-Chymotrypsin in Different Solvent Media

Kumar, Awanish; Venkatesu, Pannuru

doi:10.1021/cr2003773

Cited by 221 publications

(185 citation statements)

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“…ILs are salts composed of large organic cations and organic or inorganic anions, which contribute to a decrease on their melting temperatures. Their application as media for maintaining the protein stability has been extensively studied, either employed as co-solvents with water, in biphasic systems, or as "neat" solvents [8][9][10][11]. Some reports also demonstrated that some ILs are able to maintain or even increase the proteins stability [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Extraction and stability of bovine serum albumin (BSA) using cholinium-based Good's buffers ionic liquids

Taha

Quental

Correia

et al. 2015

Process Biochemistry

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Good's buffers ionic liquids (GB-ILs), composed of cholinium-based cations and Good's buffers anions, display self-buffering characteristics in the biological pH range, and their polarity and hydrophobicity can be easily tuned by a proper manipulation of their ions chemical structures. In this work, the extraction ability for bovine serum albumin (BSA) of aqueous biphasic systems (ABS) formed by polypropylene glycol 400 (PPG 400) and several GB-ILs was evaluated. ABS formed by PPG 400 and cholinium chloride ([Ch]Cl), GBs, and sucrose were also investigated for comparison purposes. It is shown that BSA preferentially migrates for the GB-IL-rich phase, with extraction efficiencies of 100%, achieved in a single-step. Dynamic light scattering, and circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopies were employed to evaluate the effect of the investigated cholinium-based GB-ILs on the BSA stability, and compared with results obtained for the respective GBs precursors, [Ch]Cl and sucrose, a well-known protein stabilizer. Molecular docking studies were also carried out to investigate on the binding sites of GB-IL ions to BSA. The experimental results confirm that BSA has a higher stability in GB-ILs than in any of the other compounds investigated.

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Section: Introductionmentioning

confidence: 99%

Extraction and stability of bovine serum albumin (BSA) using cholinium-based Good's buffers ionic liquids

Taha

Quental

Correia

et al. 2015

Process Biochemistry

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“…The specific surface area of BCP was one order of magnitude lower than that of activated carbon, which is used as an adsorbent, and was the pore volume of BCP was low as well. Moreover, the pore diameter peak was much smaller than the size of α-CT since the size of α-CT is 5.1 x 4.0 x 4.0 nm (Kumar & Venkatesu, 2012). Figure 1.…”

Section: Characterization Of Bamboo Charcoal Powdermentioning

confidence: 98%

“…4;2017 BCP-adsorbed α-CT was obtained by dispersing BCP in the buffer solution at pH 7 containing α-CT, and the amount of α-CT adsorbed onto BCP was 9.8 μmol/g. The charge of α-CT is positive in the buffer solution at pH 7 since the isoelectric point of α-CT is 9.1 (Kumar & Venkatesu, 2012). On the other hand, the ζ-potential of BCP is negative at pH 7 in the buffer solution at pH 7 (Noritomi et al, 2013 a ).…”

Section: Characterization Of Bamboo Charcoal Powdermentioning

confidence: 99%

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Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents

Noritomi¹,

Nishigami²,

Endo³

et al. 2017

JMSR

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We have found that the organic solvent-resistance of α-chymotrypsin (α-CT) is enhanced by adsorbing α-CT onto bamboo charcoal powder (BCP), which is obtained by pyrolyzing bamboo waste under nitrogen atmosphere, and is markedly dependent on the thermodynamic water activity (a w ) in organic solvents. When BCP-adsorbed α-CT was immersed in acetonitrile at an appropriate water activity, it effectively enhanced the transesterification of Nacetyl-L-tyrosine ethyl ester (N-Ac-Tyr-OEt) with n-butanol (BuOH) to produce N-acetyl-L-tyrosine butyl ester (N-Ac-Tyr-OBu), compared to the hydrolysis of N-Ac-Tyr-OEt with water to give N-acetyl-L-tyrosine (N-Ac-Tyr-OH). When the water activity was 0.28, the initial rate of transesterification catalyzed by BCP-adsorbed α-CT was about sixty times greater than that catalyzed by free α-CT. Regarding the reaction selectivity which is defined as a ratio of the initial rate of transesterification to that of hydrolysis, BCP-adsorbed α-CT was much superior to free α-CT. The catalytic activity of BCP-adsorbed α-CT was markedly dependent on the reaction temperature. Furthermore, concerning the thermal stability at 50 ℃, the half-life of BCP-adsorbed α-CT exhibited 3.8-fold, compared to that of free α-CT.

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“…The native structure of proteins is only marginally stable, and achieves stability/destability only within narrow ranges of conditions of co-solvent environment which can dramatically affect the protein functional activities. [8][9][10][11][12][13][14][15] It is well-known fact that even a marginal change in the natural environment around the protein may cause adverse effects on its properties. 13 The co-solvent is oen used by physical chemist or biochemist that either stabilizes or destabilizes the structures of biomolecules.…”

Section: Introductionmentioning

confidence: 99%