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Nutritional and anti-nutritional properties of lentil (Lens culinaris) protein isolates prepared by pilot-scale processing.
Joehnke, Marcel Skejovic; Jeske, Stephanie; Ispiryan, Lilit; Zannini, Emanuele; Arendt, Elke K; Bez, Jürgen; Sørensen, Jens Christian; Petersen, Iben Lykke.
Afiliação
  • Joehnke MS; Department of Food Science, University of Copenhagen, Frederiksberg, Denmark.
  • Jeske S; School of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
  • Ispiryan L; School of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
  • Zannini E; School of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
  • Arendt EK; School of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
  • Bez J; School of Food and Nutritional Sciences and APC Microbiome Institute Ireland, University College Cork, Ireland.
  • Sørensen JC; Fraunhofer-Institut für Verfahrenstechnik und Verpackung, Freising, Germany.
  • Petersen IL; Department of Food Science, University of Copenhagen, Frederiksberg, Denmark.
Food Chem X ; 9: 100112, 2021 Mar 30.
Article em En | MEDLINE | ID: mdl-33851134
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.
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Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Food Chem X Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Dinamarca

Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Food Chem X Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Dinamarca