TY - JOUR

T1 - Nutritional and anti-nutritional properties of lentil (Lens culinaris) protein isolates prepared by pilot-scale processing

AU - Joehnke, Marcel Skejovic

AU - Jeske, Stephanie

AU - Ispiryan, Lilit

AU - Zannini, Emanuele

AU - Arendt, Elke K.

AU - Bez, Jürgen

AU - Sørensen, Jens Christian

AU - Petersen, Iben Lykke

PY - 2021

Y1 - 2021

N2 - Lentil (Lens culinaris) is a high-protein crop with a promising potential as a plant-based protein source for human nutrition. This study investigated nutritional and anti-nutritional properties of whole seed lentil flour (LF) compared to lentil protein isolates (LPIs) prepared in pilot-scale by isoelectric precipitation (LPI–IEP) and ultrafiltration (LPI–UF). Fermentable oligosaccharides, disaccharides, monosaccharides, and polyols (FODMAPs) profiles showed significant reductions in total galacto-oligosaccharides (GOS) contents by 58% and 91% in LPI–IEP and LPI–UF, respectively, compared to LF. Trypsin inhibitor activity (TIA) levels based on dry protein mass were lowered by 81% in LPI–IEP and 87% in LPI–UF relative to LF. Depending on the stage of digestion, the in vitro protein digestibility (IVPD) of LPIs was improved by 35–53% compared to LF, with both products showing a similar long-term protein digestibility to that of bovine serum albumin (BSA). This work supports the use of purified LPI products as a novel source of high quality protein for food applications.

AB - Lentil (Lens culinaris) is a high-protein crop with a promising potential as a plant-based protein source for human nutrition. This study investigated nutritional and anti-nutritional properties of whole seed lentil flour (LF) compared to lentil protein isolates (LPIs) prepared in pilot-scale by isoelectric precipitation (LPI–IEP) and ultrafiltration (LPI–UF). Fermentable oligosaccharides, disaccharides, monosaccharides, and polyols (FODMAPs) profiles showed significant reductions in total galacto-oligosaccharides (GOS) contents by 58% and 91% in LPI–IEP and LPI–UF, respectively, compared to LF. Trypsin inhibitor activity (TIA) levels based on dry protein mass were lowered by 81% in LPI–IEP and 87% in LPI–UF relative to LF. Depending on the stage of digestion, the in vitro protein digestibility (IVPD) of LPIs was improved by 35–53% compared to LF, with both products showing a similar long-term protein digestibility to that of bovine serum albumin (BSA). This work supports the use of purified LPI products as a novel source of high quality protein for food applications.

KW - Alternative protein sources

KW - FODMAPs

KW - In vitro protein digestibility

KW - Lens culinaris

KW - Lentil flour

KW - Lentil protein isolates

KW - Pilot-scale processing

KW - Trypsin inhibitor activity

U2 - 10.1016/j.fochx.2020.100112

DO - 10.1016/j.fochx.2020.100112

M3 - Journal article

C2 - 33851134

AN - SCOPUS:85101318739

VL - 9

JO - Food Chemistry: X

JF - Food Chemistry: X

SN - 2590-1575

M1 - 100112

ER -