Enhanced activity of Candida antarctica lipase B in cholinium aminoate ionic liquids: a combined experimental and computational analysis ...

• Main Authors: Chan, Kam Khong, Sundaram, Vidya, Tan, Jully, Ho, Yong Kuen, Ramanan, Ramakrishnan Nagasundara, Ooi, Chien Wei
• Format: Other Non-Article Part of Journal/Newspaper
• Language: unknown
• Published: Taylor & Francis 2023
• Subjects: Biochemistry; Cell Biology; Pharmacology; Biotechnology; Chemical Sciences not elsewhere classified; Science Policy; Information Systems not elsewhere classified; Antarc*; Antarctica
• Online Access: https://dx.doi.org/10.6084/m9.figshare.24236423.v1; https://tandf.figshare.com/articles/journal_contribution/Enhanced_activity_of_i_Candida_antarctica_i_lipase_B_in_cholinium_aminoate_ionic_liquids_a_combined_experimental_and_computational_analysis/24236423/1

As a class of ionic liquids with higher biocompatibility, cholinium aminoates ([Cho][AA]) hold potential as solvation media for enzymatic bioprocessing. Herein, solvation effect of [Cho][AA] on structural stability and enzymatic activity of Candida antarctica lipase B (CALB) was evaluated using experimental and computational approaches. Influence of [Cho][AA] on CALB stability was investigated using amino acid anions ([AA] - ) with varying hydrophobicity levels. Choline phenylalaninate ([Cho][Phe]) resulted in 109.1% and 110.4% of relative CALB activity to buffer medium at 25 °C and 50 °C, respectively. Simulation results revealed the improvement of CALB’s enzymatic activities by [AA] - with a strong hydrophobic character. Shielding of CALB from water molecules by [AA] - was observed. The level of CALB activity was governed by accumulation level of [AA] - at CALB’s first hydration layer. The stronger interaction between His224 and Asp187 was postulated to be driven by [Cho][AA], resulting in the activity ...