Additive Effects of Alcohols and Polyols on Thermostability of Pepper Leaf Extracts

Abstract

Chemical chaperones (CC) are plant stress-related compounds that can stabilize protein structure in adverse environments. Modes of action are thought to involve hydrogen bonding, primarily with the solvent, and hydrophobic stabilization of the protein core. The objective of this study was to determine structure–function relationships between CC (and structurally related compounds) and thermal stability of pepper (Capsicum annuum L.) leaf proteins. Both polarity [based on log Kow (the oil–water partition coefficient)] and capacity for hydrogen bonding (based on the number of OH groups) contributed to whether low-molecular-weight alcohols and polyols stabilized or destabilized proteins at elevated temperatures. Thermal stability increased with increasing number of OH groups at a fixed number of carbon atoms per molecule. Conversely, thermal stability decreased with increasing number of carbon atoms with a fixed number of OH groups. When CC solution concentrations were adjusted to the same concentration of OH groups (1.51 × 1022 OH groups per milliliter), protein thermal stability increased with increasing CC polarity. Mixtures of different CC had additive effects on increasing protein thermostability, but mixtures of stabilizing (mannitol) and destabilizing (methanol) compounds negated each other. As a strategy for increasing plant thermotolerance, identification and removal of destabilizing compounds should be equally effective as increasing levels of stabilizers in protecting protein conformation at elevated temperatures.