Nutritional and anti-nutritional properties of lentil (Lens culinaris) protein isolates prepared by pilot-scale processing
Autor: | Iben Lykke Petersen, Elke K. Arendt, Jens Christian Sørensen, Emanuele Zannini, Marcel Skejovic Joehnke, Lilit Ispiryan, Jürgen Bez, Stephanie Jeske |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
TNBS
trinitrobenzenesulfonic acid Lens culinaris LPC(s) lentil protein concentrate(s) PD protein digestibility Pilot-scale processing MW(s) molecular weight(s) TIU trypsin inhibitor unit Alternative protein sources Analytical Chemistry DH degree of hydrolysis LF(s) lentil flour(s) AA amino acids E:S ratios enzyme:substrate ratios IVPD % in vitro protein digestibility Food science LPI–UF lentil protein isolate prepared by UF Bovine serum albumin ANOVA analysis of variance chemistry.chemical_classification lentil flour lentil protein isolates alternative protein sources pilot-scale processing trypsin inhibitor activity in vitro protein digestibility FODMAPs biology lcsh:TP368-456 IVPD PT % 1+1 h short-term protein digestibility IVPD PT % 1+3 h medium-term protein digestibility DM dry matter LP lentil protein(s) ANC(s) anti-nutritional compound(s) RFO raffinose family oligosaccharides FOS Fructans and fructo-oligosaccharides Digestion LPI–IEP lentil protein isolate prepared by IEP lcsh:Nutrition. Foods and food supply IEP isoelectric precipitation Research Article LPI(s) lentil protein isolate(s) IBS irritable bowel syndrome IVPD P % pepsin digestibility Ultrafiltration lcsh:TX341-641 l–BAPA N–α–benzoyl–l–arginine–4–nitroanilide TCA trichloroacetic acid TIA trypsin inhibitor activity UF ultrafiltration Monosaccharide In vitro protein digestibility GOS galacto-oligosaccharides Lentil protein isolates OPA o-phthaldialdehyde Pilot scale IVPD PT % 1+24 h long-term protein digestibility HPAEC-PAD high performance anion exchange chromatography coupled with pulsed amperometric detection lcsh:Food processing and manufacture Isoelectric point Human nutrition Trypsin inhibitor activity chemistry Lentil flour biology.protein TU trypsin activity unit FODMAPs fermentable oligo- di- and monosaccharides and polyols Food Science |
Zdroj: | Food Chemistry: X, Vol 9, Iss, Pp 100112-(2021) Food Chemistry: X Joehnke, M S, Jeske, S, Ispiryan, L, Zannini, E, Arendt, E K, Bez, J, Sørensen, J C & Petersen, I L 2021, ' Nutritional and anti-nutritional properties of lentil ( Lens culinaris ) protein isolates prepared by pilot-scale processing ', Food Chemistry: X, vol. 9, 100112 . https://doi.org/10.1016/j.fochx.2020.100112 |
ISSN: | 2590-1575 |
DOI: | 10.1016/j.fochx.2020.100112 |
Popis: | Highlights • Two lentil protein isolates (LPIs) and a lentil flour (LF) were prepared in pilot-scale. • Nutritional and anti-nutritional properties of LPIs were examined in comparison to LF. • Total galacto-oligosaccharides (GOS) contents of LPIs were reduced by 58–91%. • Trypsin inhibitor activity (TIA) levels of LPIs were reduced by 81–87%. • In vitro protein digestibility (IVPD) values of LPIs were improved by 35–53%. 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. |
Databáze: | OpenAIRE |
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