Nonspecific lipid transfer proteins (LTPs) were first isolated from potato tubers and identified by Kader (1975). LTPs are ubiquitous small proteins (molecular weights ranging from 6.5 to 10 kDa) that exist in all terrestrial plants (Salminen et al., 2016). They have eight cysteine residue motifs that form four conserved disulphide bridges, which help stabilize the peptide tertiary structure, and many α-helices with a central hydrophobic cavity capable of binding to a variety of lipids such as fatty acids, fatty acyl-CoA, phospholipids, and prostaglandin B2 (Madni et al., 2020;Salminen et al., 2016). LTPs are encoded by large gene families and expressed abundantly in a variety of plant tissues. Almost all nonspecific LTPs carry an N-terminal signal that localizes the protein at the subcellular level (Edstam et al., 2011;Missaoui et al., 2022). Traditionally, LTPs are classified according to molecular weight or sequence identity (Boutrot et al., 2008;Kalla et al., 1994). A more recent classification system by Edstam et al. (2011) uses five major types (LTP1, LTP2, LTPc, LTPd and LTPg) and five minor types (LTPe, LTPf, LTPh, LTPj and LTPk) based on the position of a conserved intron, the amino acid sequence identity, and posttranslational modifications. Expression of many nonspecific LTPs can be induced by multiple biotic and abiotic stresses, including