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
N1 - Publisher Copyright:
© 2021 The Authors
PY - 2021/3/30
Y1 - 2021/3/30
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
UR - https://www.scopus.com/pages/publications/85101318739
U2 - 10.1016/j.fochx.2020.100112
DO - 10.1016/j.fochx.2020.100112
M3 - Article
AN - SCOPUS:85101318739
VL - 9
JO - Food Chemistry: X
JF - Food Chemistry: X
M1 - 100112
ER -