Research output: Contribution to journal › Article › peer-review
Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Effect of uni-divalent electrolyte in the interaction associated with solubility for the predominant form of L-isoleucine and L-serine in aqueous media
AU - Ghosh, Biplab
AU - Chowdhury, Saroj
AU - Sing, Nilam
AU - Mondal, Pratima
AU - Mondal, Mrinmay
AU - Hansda, Bharat Chandra
AU - Roy, Sanjay
AU - Henaish, A. M. A.
AU - Ahmed, Jahangeer
AU - Mahali, Kalachand
N1 - Dr. Roy extends his appreciation to the Netaji Subhas Open University for the generous financial aid provided to carry out the ongoing research. The assistance was granted through Project Office Order No: AC/140/2021-22 dated 01/11/2021 and Project No. Reg/1290 dated 22-11-2021. KM expresses gratitude to the Science & Technology and Biotechnology, (W.B.), Project No: ST/P/S&T/15g-5/2018, and the DST-FIST Level –II Govt. of India for the financial support received at the Department of Chemistry, Kalyani University. JA acknowledges the Researchers Supporting Project number (RSP2023R391) at King Saud University, Riyadh, Saudi Arabia to support this research
PY - 2023
Y1 - 2023
N2 - The study aimed to measure the solubilities of L-serine and L-isoleucine in an aqueous ammonium sulfate [(NH4)2SO4] solution at different temperatures (288.15 to 308.15 K) using a gravimetric technique. In pure aqueous media L-serine solubility is 4.1218 in mol•kg−1 of water while for L-isoleucine is 0.3094 mol•kg−1 at 298.15 K. The obtained solubility data was used to estimate the thermodynamic properties of the amino acids, such as the standard Gibbs free energy and standard entropy change during the solvation process. The analysis involved investigating the short range chemical interactions between the amino acids and the electrolyte solution, which significantly influenced the solvation thermodynamics. The study found that L-serine exhibited a salting in effect, meaning its solubility increased in the presence of ammonium sulfate, while L-isoleucine experienced a salting out effect, resulting in decreased solubility with the electrolyte. Additionally, solubility parameters were employed to assess the chemical strength of the amino acids and understand their solute–solvent interactions and relative solubilities in the solution. Overall, this experimental investigation provided valuable insights into the solvation behavior and chemical characteristics of L-serine and L-isoleucine in the presence of an electrolyte solution.
AB - The study aimed to measure the solubilities of L-serine and L-isoleucine in an aqueous ammonium sulfate [(NH4)2SO4] solution at different temperatures (288.15 to 308.15 K) using a gravimetric technique. In pure aqueous media L-serine solubility is 4.1218 in mol•kg−1 of water while for L-isoleucine is 0.3094 mol•kg−1 at 298.15 K. The obtained solubility data was used to estimate the thermodynamic properties of the amino acids, such as the standard Gibbs free energy and standard entropy change during the solvation process. The analysis involved investigating the short range chemical interactions between the amino acids and the electrolyte solution, which significantly influenced the solvation thermodynamics. The study found that L-serine exhibited a salting in effect, meaning its solubility increased in the presence of ammonium sulfate, while L-isoleucine experienced a salting out effect, resulting in decreased solubility with the electrolyte. Additionally, solubility parameters were employed to assess the chemical strength of the amino acids and understand their solute–solvent interactions and relative solubilities in the solution. Overall, this experimental investigation provided valuable insights into the solvation behavior and chemical characteristics of L-serine and L-isoleucine in the presence of an electrolyte solution.
UR - http://www.scopus.com/inward/record.url?partnerID=8YFLogxK&scp=85164290175
UR - https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=tsmetrics&SrcApp=tsm_test&DestApp=WOS_CPL&DestLinkType=FullRecord&KeyUT=001038729300001
U2 - 10.1016/j.molliq.2023.122432
DO - 10.1016/j.molliq.2023.122432
M3 - Article
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
SN - 0167-7322
IS - 385
M1 - 122432
ER -
ID: 41986361