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hemp seed protein

Chapter 7 – Hemp Seed (Cannabis sativa L.) Proteins : Composition, Structure, Enzymatic Modification, and Functional or Bioactive Properties

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Abstract

Hemp (Cannabis sativa L.) is a source of nutritious seeds that have been used as human food for thousands of years. The seeds contain nonmedicinal levels ( 70% solubility at pH 4.0–6.0, whereas most plant proteins are typically insoluble. Addition of hemp seed protein to polycystic kidney disease rat diet led to reduced pathological intensity of renal disease and amelioration of associated cardiovascular impairment. Moreover, hemp seed enzymatic hydrolysates have proven effective during in vitro and in vivo tests as antioxidant and antihypertensive agents. Therefore, hemp seed proteins and hydrolysates have the potential to be used as ingredients to formulate functional foods.

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Chapter 7 – Hemp Seed ( Cannabis sativa L.) Proteins : Composition, Structure, Enzymatic Modification, and Functional or Bioactive Properties Add to Mendeley Abstract Hemp ( Cannabis

Structural and functional properties of hemp seed protein products

Affiliation

  • 1 Dept. of Human Nutritional Sciences, Univ. of Manitoba, Winnipeg, Manitoba, R3T 2N2, Canada.
  • PMID: 25048774
  • DOI: 10.1111/1750-3841.12537

Structural and functional properties of hemp seed protein products

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Authors

Affiliation

  • 1 Dept. of Human Nutritional Sciences, Univ. of Manitoba, Winnipeg, Manitoba, R3T 2N2, Canada.
  • PMID: 25048774
  • DOI: 10.1111/1750-3841.12537

Abstract

The effects of pH and protein concentration on some structural and functional properties of hemp seed protein isolate (HPI, 84.15% protein content) and defatted hemp seed protein meal (HPM, 44.32% protein content) were determined. The HPI had minimum protein solubility (PS) at pH 4.0, which increased as pH was decreased or increased. In contrast, the HPM had minimum PS at pH 3.0, which increased at higher pH values. Gel electrophoresis showed that some of the high molecular weight proteins (>45 kDa) present in HPM were not well extracted by the alkali and were absent or present in low ratio in the HPI polypeptide profile. The amino acid composition showed that the isolation process increased the Arg/Lys ratio of HPI (5.52%) when compared to HPM (3.35%). Intrinsic fluorescence and circular dichroism data indicate that the HPI proteins had a well-defined structure at pH 3.0, which was lost as pH value increased. The differences in structural conformation of HPI at different pH values were reflected as better foaming capacity at pH 3.0 when compared to pH 5.0, 7.0, and 9.0. At 10 and 25 mg/mL protein concentrations, emulsions formed by the HPM had smaller oil droplet sizes (higher quality), when compared to the HPI-formed emulsions. In contrast at 50 mg/mL protein concentration, the HPI-formed emulsions had smaller oil droplet sizes (except at pH 3.0). We conclude that the functional properties of hemp seed protein products are dependent on structural conformations as well as protein concentration and pH.

Keywords: circular dichroism; emulsion; hemp seed; intrinsic fluorescence; protein functionality.

The effects of pH and protein concentration on some structural and functional properties of hemp seed protein isolate (HPI, 84.15% protein content) and defatted hemp seed protein meal (HPM, 44.32% protein content) were determined. The HPI had minimum protein solubility (PS) at pH 4.0, which increase …