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
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
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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