Effect of extraction method on functional properties of flaxseed protein concentrates

Tirgar, Mina; Silcock, Patrick; Carne, Alan; Birch, E. John

doi:10.1016/j.foodchem.2016.08.002

Cited by 102 publications

(55 citation statements)

References 36 publications

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“…Avramenko et al (2013) reported DH to have no significant effect on the zeta potential of a lentil protein isolate (~−35 mV) treated with trypsin up to 10% DH (~−38 mV). Compared with the literature, the surface charge of untreated PPEF was lower than that of pea protein isolate (~91% protein; −24 mV; Lam et al, 2017) but comparable to a pea protein concentrate (73% protein; −16 mV; Tirgar, Silcock, Carne, & Birch, 2017), indicating that the carbohydrates and minerals present in the sample may screen charges on the protein. It is hypothesized that the positively charged ash in the PPEF could shield the electrical double layer on the protein and the carbohydrate in the sample can give rise to starch-protein interactions when the PPEF is in solution, reducing the overall charge of the PPEF as compared to a much purer protein sample.…”

Section: Surface Characteristicscontrasting

confidence: 67%

Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

et al. 2019

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Background and objectives Air‐classified pea protein‐enriched flour (PPEF) was modified with trypsin, Savinase, papain, and pepsin to achieve 2%–4% and 10%–12% degrees of hydrolysis, and the surface and functional properties of the hydrolyzed products were assessed. Findings Surface hydrophobicity increased from 13.3 to 48.5 A.U. with papain treatment. Surface charge became more electronegative from −12.6 to −19.0 mV with pepsin treatment. However, solubility of hydrolyzed PPEF at all pH values tested (4.0, 7.0, and 10.0), regardless of enzyme treatment, decreased. Low solubility of hydrolyzed proteins negatively impacted solubility‐dependant functional properties: foaming properties and emulsifying properties decreased. However solubility‐independent properties (water‐ and oil‐holding capacity; WHC and OHC, respectively) improved with proteolysis, increasing from 0.6 g/g to 1.4–2.0 g/g and from 0.7 g/g to 1.0–1.5 g/g, respectively. Conclusions Papain treatment yielded the best results in terms of both OHC and WHC of PPEF. Significance and novelty The resultant hydrolyzates have potential for baked goods and processed meat applications because of their increased OHC and WHC.

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Section: Surface Characteristicscontrasting

confidence: 67%

Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

et al. 2019

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“…The ESO was recorded to be 96.25% for WSP and 85.29% for SPO, respectively. The EAO of WSP and SPO was found to be 77.57 m 2 /g and 56.72 m 2 /g, respectively, which was higher than that of Torreya grandis seed protein (44.57 m 2 /g) (Yu et al, 2017) and rice bran protein (10.28 m 2 /g) (Phongthai et al, 2016), but lower than that of flaxseed protein (87.10 m 2 /g) (Tirgar et al, 2017) and Kiwi fruit seed protein (92.38.10 m 2 /g) (Deng et al, 2014). The reasons for the higher EAO and ESO in WSP compared to SPO were that the relatively more hydrophobic groups on WSP molecules improved the hydrophilic-lipophilic balance and formed the stable interfacial layer for better emulsification activity (Jain & Anal, 2016;Phongthai et al, 2016), which was confirmed by the higher DHC of WSP.…”

Section: Emulsifying Propertiesmentioning

confidence: 73%

Ultrasonic-assisted extraction and functional properties of wampee seed protein

Liu

et al. 2019

Food Sci. Technol

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The wampee seed protein (WSP) was extracted by the ultrasonic and alkaline solution. Response surface methodology was used to optimize the extraction parameters for obtaining the highest protein yield, and the protein's functional properties such as protein solubility, water and oil holding capacity, and emulsifying and foaming properties ware studied in comparison with soy protein isolate (SPO). The results showed that ultrasonic time and pH significantly influenced the yield, and the optimal extraction conditions were achieved when solid-solvent ratio, ultrasonic time and pH were 1:29 g/mL, 64 min and 12, respectively, under which the yield was 15.06%. The functional property tests revealed that the WSP's solubility was higher than that of SPO and its isoelectric point was near 3.0. Compared with SPO, the oil holding capacity, emulsion activity index and emulsion stability index of WSP were significantly higher, but its water holding capacity, foaming capacity and foaming stability were significantly lower.Practical Application: The optimal extraction conditions for wampee seed protein are desirable and practical, and the wampee seed protein can be used as a new protein source for its functional properties. Liu et al.

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“…The emulsifying activity (EAI) and stability (ESI) of SCGs and SCGPI were estimated according to the methods of Tirgar, Silcock, Carne, and Birch () with slightly modification. Each sample was dissolved in distilled water at 0.2% (wt/vol), adjusted to pH 3.0–8.0 by using 1 mol/L HCl or 1 mol/L NaOH.…”

Section: Methodsmentioning

confidence: 99%

Physicochemical and functional properties of protein isolate from sea cucumber ( Stichopus japonicus ) guts

Guo

Han

et al. 2019

J Food Process Preserv

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Protein isolate of sea cucumber guts (SCGPI) was extracted from defatted power of sea cucumber guts (SCGs) by alkaline extraction and acid precipitation method. The physicochemical and functional properties of SCGPI were evaluated in comparison with those of SCGs. It was found that the SCGPI showed higher whiteness, and contained 39.5% of the essential amino acids with higher protein efficiency ratio. The functionalities of SCGPI, including solubility, water/oil holding capacity (WHC/OHC), foaming capacity (FC), and emulsifying abilities (EAI), were significantly higher than those of SCGs. SCGPI exhibited higher total sulfhydryl group, disulfide bond, β‐turns, and random coil, while less surface hydrophobicity and α‐helix than SCGs. The thermal denaturation temperature of SCGPI was 46.55°C and the microstructure of SCGPI was flaky. Moreover, OHC, FC, and EAI of SCGPI were significantly better than those of SPI. These results suggest SCGPI can be used as functional bases in the food industry. Practical applications Sea cucumber (Stichopus japonicus) guts are the main byproducts in the sea cucumber processing, which are rich in protein. In this study, we prepared protein isolate from sea cucumber guts (SCGPI) by alkaline extraction and acid precipitation method. The results showed that SCGPI exhibited great solubility, water/oil holding capacity, foaming capacity, and emulsifying abilities. The present study demonstrates that SCGPI can be used as a functional base in the food industry.

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Effect of extraction method on functional properties of flaxseed protein concentrates

Cited by 102 publications

References 36 publications

Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

Ultrasonic-assisted extraction and functional properties of wampee seed protein

Physicochemical and functional properties of protein isolate from sea cucumber ( Stichopus japonicus ) guts

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