Structural Modification of Jackfruit Leaf Protein Concentrate by Enzymatic Hydrolysis and Their Effect on the Emulsifier Properties

Abstract

Jackfruit leaf protein concentrate (LPC) was hydrolyzed by pepsin (H–Pep) and pancreatin (H–Pan) at different hydrolysis times (30–240 min). The effect of the enzyme type and hydrolysis time of the LPC on the amino acid composition, structure, and thermal properties and its relationship with the formation of O/W emulsions were investigated. The highest release of amino acids (AA) occurred at 240 min for both enzymes. H–Pan showed the greatest content of essential and hydrophobic amino acids. Low β-sheet fractions and high β-turn contents had a greater influence on the emulsifier properties. In H–Pep, the β-sheet fraction increased, while in H–Pan it decreased as a function of hydrolysis time. The temperatures of glass transition and decomposition were highest in H–Pep due to the high content of β-sheets. The stabilized emulsions with H–Pan (180 min of hydrolysis) showed homogeneous distributions and smaller particle sizes. The changes in the secondary structure and AA composition of the protein hydrolysates by the effect of enzyme type and hydrolysis time influenced the emulsifying properties. However, further research is needed to explore the use of H–Pan as an alternative to conventional emulsifiers or ingredients in functional foods.

Optimization of Water Lentil (Duckweed) Leaf Protein Purification: Identification, Structure, and Foaming Properties

“…Thermal analyses were performed with a TA instrument DSC Q1000 (TA Instruments, New Castle, DE, USA), with a nitrogen flow of 50 mL/min and a pressure of around 20 PSI in the nitrogen cylinder. The protocol was adapted from Martin et al [ 26 ] and Calderón-Chiu et al [ 56 ], with some modifications. Indium in a non-hermetic coated aluminum pan was used as calibration, and an empty non-hermetic pan was used as reference.…”

“…Indium in a non-hermetic coated aluminum pan was used as calibration, and an empty non-hermetic pan was used as reference. About 2.5–8 mg of samples [ 56 ] (containing between 20% and 57% protein) were weighed in non-hermetic pans and then sealed with the appropriate lids using a sample encapsulation press (TA Instruments, New Castle, DE, USA). The temperature scans were performed from 10 °C to 200 °C in linear mode at a rate of 2 °C/min [ 26 ].…”

Functional, physicochemical, and rheological properties of the spray drying particles prepared from the noble scallop (Chlamys nobilis) mantle protein‐pectin hydrated mixtures

“…2d); thus, indicating that an excellent compatibility between the protein and pectin (Lavaei et al ., 2022). The T d of AP (84.75 ± 0.85 °C) was higher when compared with HP (72.97 ± 2.70 °C), which could be speculated that more heat‐vulnerable secondary structures of a protein such as α‐helices, loops, and random coils changing to β‐sheets during the enzymatic hydrolysis, as large sections of a protein consisting predominantly of β‐sheets contributed to the excellent thermal stabilities of peptides (Calderón‐Chiu et al ., 2022). Thermal stability of protein‐pectin spray drying particles significantly improved compared with HP or AP, respectively.…”

Nutritional Profile, Antinutritional Factors, and Digestibility of Proteins in Non-conventional Leaf Protein Sources

“…The kind of amino acids that can be made available also partly depends on the type of enzyme hydrolyzing it and up-to what time. A study reported that pancreatin exhibited a greater degree of hydrolysis (DH) (6.12–9.21%) than pepsin, which showed a DH of 1.78–3.44%, thus explaining the larger content of amino acids in the pancreatin-hydrolyzed LPC …”

“…A study reported that pancreatin exhibited a greater degree of hydrolysis (DH) (6.12−9.21%) than pepsin, which showed a DH of 1.78− 3.44%, thus explaining the larger content of amino acids in the pancreatin-hydrolyzed LPC. 45 The kind of extraction methods employed to obtain LPC also affects its amino acid composition. Higher levels of lysine, sulfurated amino acids, threonine, and tryptophan concentrations were achieved by using an ultrafiltration-assisted extraction method than using an acid thermo-coagulationassisted extraction method.…”