Hempseed protein has gained increasing attention for its sustainability and nourishment. This study aimed to investigate the effects of spray drying and freeze drying on the physicochemical properties, functionality, and digestibility of hempseed protein isolate (HPI). Compared to undried-HPI, both drying techniques altered physicochemical and structural properties. Particularly, protein denaturation temperature increased in freeze-dried HPI (FD-HPI) and spray-dried HPI (SD-HPI) samples (∼90 °C) than in undried-HPI (82.5 °C). Lysine content decreased from 38.26 mg/g in undried-HPI to 35.03 and 33.18 mg/g in FD-HPI and SD-HPI, respectively. Results revealed the loss of 26 and 17 kDa bands after drying. Notably, FD-HPI exhibited higher emulsifying stability and oil-holding capacity than SD-HPI. While both FD-HPI and SD-HPI had higher digestibility than undried-HPI, a 50% reduction in the liberation of free α-amino groups after digestion was found. This study provided information regarding changes in HPI after drying, offering insights for HPI production and application in the food industry.

This study evaluates the effects of alkaline and micellisation extraction methods, alongside freeze-drying and spray-drying, on the protein subunits, amino acid profiles, and proteome data of hempseed protein isolate (HPI). Findings revealed that the extraction methods affect protein profiles more than the drying methods. Micellisation-extracted HPI showed higher albumin, oleosin, and sulphur-containing protein levels than alkaline-extracted HPI. The alkali-extracted undried sample (AU) gave more potentially allergenic proteins, including Hsp70 and triosephosphate isomerase, than its micellization-extracted counterpart (MU). Unique potential allergens were identified, including malate dehydrogenase and enolase in AU, and RuBisCo in MU samples. Both drying processes impacted the HPI proteome and reduced RuBisCo in the micellisation-extracted HPI. These insights highlight the crucial role of method selection in HPI processing for optimising production in the food industry.

This study investigated the physicochemical properties, functionalities, and antioxidant capacities of protein extracts from wild sea cucumber Australostichopus mollis collected from four distinct locations in New Zealand. Protein was extracted from sea cucumber body walls using trypsin enzymatic extraction, followed by cold acetone precipitation. The amino acid analysis revealed high glycine (189.08 mg/g), glutamic acid (119.45 mg/g), and aspartic acid (91.91 mg/g) concentrations in all samples. The essential amino acid indexes of the protein extracts (62.96, average) were higher than the WHO/FAO standard references, indicating the excellent protein quality of A. mollis. Furthermore, protein extracts from A. mollis demonstrated superior emulsifying activity (202.3–349.5 m²/g average) compared to commercial soy and whey protein isolates under all tested pH conditions, and enhanced foaming capacity (109.9–126.4%) and stability (52.7–72%) in neutral and acidic conditions. The extracts also exhibited good solubility, exceeding 70% across pH 3–11. Antioxidant capacities (ABTS and DPPH free radical scavenging activity and ferric reducing antioxidant power) were identified in A. mollis protein extracts for the first time, with clear variations observed among different locations. These findings elucidate the advantageous functional properties of protein extracts from wild New Zealand A. mollis and highlight their potential application as high-quality antioxidant food ingredients.

This study demonstrated a comprehensive workflow combining in silico screening and prediction with in vitro validation to investigate the bioactivity of hempseed protein isolate (HPI) extracted and dehydrated using different methods. By adopting an in silico approach, 13 major proteins of HPI were hydrolysed by 20 selected enzymes, leading to the prediction of 20 potential bioactivities. With papain hydrolysis, dipeptidyl peptidase-IV (DPP4) and angiotensin-converting enzyme (ACE) inhibitory activities emerged as having the highest potential. In vitro experiments confirmed these predictions, with DPP4 and ACE inhibitory activities displaying IC50 values of 0.32-0.42 mg/mL and 6.8-9.17 mu g/mL, respectively. A strong correlation (r2 2 = 0.96) was observed between in vitro protein inhibitory results and in silico predicted data. This study demonstrated an effective integrative approach for predicting bioactive peptides in food protein, providing valuable guidance on its processing to create value-added products.