Physicochemical, Structural, and Functional Properties of Hemp Protein vs Several Commercially Available Plant and Animal Proteins: A Comparative Study

Abstract

The physicochemical, structural, and functional properties of hemp seed protein were investigated and compared with soy, pea, whey, and egg proteins. Hemp protein exhibited the lowest total (67.1 g/100 g) and essential amino acid contents (23.1 g/ 100 g) but the highest arginine level (9.17 g/100 g). Hemp protein had a β-sheet conformation as the predominant secondary structure and demonstrated four major bands located at ∼18, ∼20, and ∼34−36 kDa in an SDS-PAGE profile, corresponding to the basic and acidic subunits of edestin, respectively. The highly compact structure of hemp protein along with a higher surface hydrophobicity (H 0 ) of 750 × 10 4 au and −SH content of 34.85 μmol/g may explain the low water absorption capacity (372.41 g/ 100 g) and protein solubility, but a high oil absorption capacity (135.48 g/100 g) and emulsification activity index of 48.40 m 2 /g are found. Our results support the potential use of hemp protein in various protein-rich food products. However, appropriate processing technologies are needed to modify its structure and functionality.

Bromelain Hydrolysis Modified the Functionality, Antioxidant, and Anti-Inflammatory Properties of Hempseed (Cannabis sativa L.) Protein Isolated at pH 12

“…Xu et al. also viewed high H 0 values and low PS of hempseed proteins, identifying strong protein–protein interactions that form insoluble aggregates in addition to the highly disulfide-bonded native structure to contribute to low PS and high H 0 values . Our measurement of high HPI-12 H 0 is further supported by the above measurement of protein solubility, whose relative solubility improved at all pH values for BHPI-12, resulting from hydrolysis releasing peptides with a lesser degree of hydrophobic interaction in aqueous environments.…”

Impact of Topography on Soil Properties in Delboatwaro Subwatershed, Southern Ethiopia

“…The landscape of the study area had influenced soil formation, with soils on the higher slopes being developed by in situ weathering of parent material, where continuous deposition of materials from the upper slope led to the development of different soil types on the lower slopes [63,64]. The main threats to increasing agricultural production at three sites in the DelboAtwaro subsea catchment on a reasonable basis are low organic carbon, total nitrogen was rated from low to medium; available phosphorus ranged from very low to low; optimal in copper and iron; very high in a manganese and exchangeable potassium was varied from very low to optimal [62,65]. Magnesium-related depletions of basic cations, particularly K and to a lesser extent Ca, are expected in soils at various topographical locations.…”

Structural and Functional Properties of Kabuli Chickpea Protein as Affected by High Hydrostatic Pressures

“…Defatted flour (1:5, w/v) was dispersed in distilled water and adjusted to pH 9.5 using 0.1 N NaOH. The dispersion was stirred for 1 h at the room temperature and then centrifuged at 4500 g for 20 min at 4 °C, as described by Xu et al The supernatant was then decanted and adjusted to pH 4.5 using HCl (1 N) to precipitate protein. The precipitated proteins were further recovered by centrifugation at 4500 g for 20 min at 4 °C followed by washing twice using distilled water (1:10 w/v) and centrifuging at 4500 g for 10 min.…”

“…A Varian 640 Fourier Transform Infrared Spectrometer (FTIR, Agilent Technologies, Santa Clara, CA) was used to evaluate the protein secondary structure, as described in our previous study . The protein samples were compressed onto a single-reflection universal ATR platform (Pike Technologies MIRacle ATR, Madison, WI) and then scanned from 400 to 4000 cm –1 at 4 cm –1 resolution with 30 scans averaged.…”

“…1-Anilino-8-naphthalenesulfonate (ANS) was used as a hydrophobic fluorescence probe to determine the H 0 , as previously described by Xu et al Soluble protein was obtained by dissolving protein isolates in 10 mM phosphate buffer (pH 7.0) with stirring overnight at room temperature followed by centrifugation at 4,500 g at 20 min. Protein concentrations of the supernatants were determined by a Pierce 660 nm Protein Assay with bovine gamma globulin (Thermo Fisher Scientific, Waltham, MA) as a standard.…”