Quality of Lupinus albus L. (White Lupin) Seed: Extent of Genotypic and Environmental Effects

White lupin seed can be used for traditional and functional foods or as animal feed. This study aimed to support lupin breeders and production stakeholders by assessing the extent of genotypic, environmental, and genotype × environment (GE) interaction effects on seed contents of oil, tocopherols (TOC), and quinolizidine alkaloids (QA), grain yield, and seed weight of eight elite genotypes grown in two climatically contrasting Italian locations for two cropping years. On average, plants in the subcontinental climate site exhibited higher grain yield and seed size, about 8% lower oil content, and almost 85% higher QA content than those in the Mediterranean climate site. The range of genotype means was 2.97–5.14 t/ha for yield, 92–110 mg/g for oil, and 0.121–0.133 mg/g for TOC. TOC amount was largely unpredictable and featured large GE interactions that hinder its genetic improvement. Oil and alkaloid contents and seed size are more predictable and offer potential for selection

Exploration of Potentially Bioactive Peptides Generated from the Enzymatic Hydrolysis of Hempseed Proteins

The seed of industrial hemp is an underexploited protein source. In view of a possible use in functional foods, a hempseed protein concentrate was hydrolyzed with pepsin, trypsin, pancreatin, or a mixture of these enzymes. A detailed peptidomic analysis using data-dependent acquisition showed that the numbers of peptides identified ranged from 90 belonging to 33 parent proteins in the peptic hydrolysate to 9 belonging to 6 proteins in the pancreatin digest. The peptic and tryptic hydrolysates resulted to be the most efficient inhibitors of 3-hydroxymethyl-coenzyme A reductase activity when tested on the catalytic domain of the enzyme. Using the open access tools PeptideRanker and BIOPEP, a list of potentially bioactive peptides was generated: the alleged activities included the antioxidant property, the glucose uptake stimulating activity, the inhibition of dipeptidyl peptidase-IV and angiotensin-converting enzyme I

New ACE-Inhibitory Peptides from Hemp Seed (<i>Cannabis sativa</i> L.) Proteins

A hemp seed protein isolate, prepared from defatted hemp seed meals by alkaline solubilization/acid precipitation, was subjected to extensive chemical hydrolysis under acid conditions (6 M HCl). The resulting hydrolysate was fractionated by semipreparative RP-HPLC, and the purified fractions were tested as inhibitors of angiotensin converting enzyme (ACE). Mono- and bidimensional NMR experiments and LC-MS analyses led to the identification of four potentially bioactive peptides, i.e. GVLY, IEE, LGV, and RVR. They were prepared by solid-phase synthesis, and tested for ACE-inhibitory activity. The IC₅₀ values were GVLY 16 ± 1.5 μM, LGV 145 ± 13 μM, and RVR 526 ± 33 μM, confirming that hemp seed may be a valuable source of hypotensive peptides