Biochimica et Biophysica Acta (BBA) - Protein Structure
Studies on Brassica seed proteins: I. The low molecular weight proteins in rapeseed. Isolation and characterization
References (15)
- et al.
Can. Inst. Food Technol. J.
(1970) Chromatogr. Rev.
(1967)- et al.
Arch. Biochem. Biophys.
(1969) - et al.
Biochim. Biophys. Acta
(1967) - et al.
J. Biol. Chem.
(1969) FEBS Lett.
(1971)
Cited by (104)
Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation
2023, Food Chemistry AdvancesCruciferin versus napin – Air-water interface and foam stabilizing properties of rapeseed storage proteins
2023, Food HydrocolloidsCitation Excerpt :Understanding the characteristics of the different protein families is crucial to allow effective applications (E. Ntone et al., 2021). Rapeseed proteins mainly consist of two storage protein groups: cruciferin and napin (Crouch & Sussex, 1981; Lönnerdal & Janson, 1972). Cruciferin belongs to the 11S globulin class, which is soluble in dilute salt solution, while napin belongs to the water-soluble 2S albumins.
Monitoring food structure in plant protein gels during digestion: Rheometry and Small Angle Neutron Scattering studies
2022, Food StructureCitation Excerpt :These two proteins differ from each other by their molecular weights and their IEP values. Cruciferin is a hexamer (~ 300 kDa), containing an α-(acidic) and a β-(basic) chain in each unit, giving the IEP of the molecule in the neutral pH ~ 7 (Schwenke, Raab, Linow, Pahtz, & Uhlig, 1981; Schwenke, Raab, Plietz, & Damaschun, 1983) (other authors reported however different IEP values in the pH range from 4 to 8 (Lönnerdal and Janson, 1972; Pedroche et al., 2004)). In comparison, napin is much smaller (~ 14 kDa) and basic, 2-chain protein, with the IEP at the pH ~ 11 (Bérot, Compoint, Larré, Malabat, & Guéguen, 2005; Espert et al., 2016; Shewry, Napier, & Tatham, 1995).
Dispersion stability of non-refined turnip rapeseed (Brassica rapa) protein concentrate: Impact of thermal, mechanical and enzymatic treatments
2016, Food and Bioproducts ProcessingCitation Excerpt :The main storage proteins cruciferin and napin constitute 60% and 20% of the total protein, respectively in canola/rapeseed (Aider and Barbana, 2011). Cruciferin (12S globulin) shows an isoelectric point (pI) at the range of pH 4–7 (Schwenke et al., 1980; Bérot et al., 2005) whereas napin (2S albumin) is a basic protein with pI > 10 (Lönnerdal and Janson, 1972). The different isoelectric points between cruciferin and napin could not be distinguished in the monomodal charge distributions.
A new way for the oil plant biomass valorization: Polyphenols and proteins extraction from rapeseed stems and leaves assisted by pulsed electric fields
2015, Industrial Crops and ProductsCitation Excerpt :Table 3 shows that low pH value (pH 2) resulted in high polyphenols yield, while proteins have a statistically better solubility at neutral pH. Lower solubility of proteins at acid and alkaline pH can be explained by their isoelectric points. Lonnerdal and Janson (1972) suggested that a large proportion of canola proteins (20–40%) have isoelectric points close to pH 11, while the other proteins have isoelectric points spread out in the interval of pH 4–8. All the following experiments are going to be conducted at neutral pH in order to obtain relatively high protein yield.
Proteomic identification of allergenic seed proteins, napin and cruciferin, from cold-pressed rapeseed oils
2015, Food ChemistryCitation Excerpt :Major allergens (Bra n 1 and Bra r 1, respectively) were identified as 2S albumins; napins that are seed storage proteins in both of these oil plants (Puumalainen et al., 2006) and represent approximately 20% of the total protein. Napin, consisting of a small and large chain linked by disulphide bonds (Lonnerda & Janson, 1972), is reported to be extremely resistant to pepsin digestion and denaturation caused by heat and low pH (Murtagh et al., 2003). Thus it is possible that napin is not destroyed during conventional food processing.