Alkali solution extraction of rice residue protein isolates: Influence of alkali concentration on protein functional, structural properties and lysinoalanine formation

Hou, Furong; Ding, Wenhui; Qu, Wenjuan; Oladejo, Ayobami Olayemi; Feng, Xiaohua; Zhang, Weiwei; He, Ronghai; Ma, Haile

doi:10.1016/j.foodchem.2016.09.064

Cited by 185 publications

(104 citation statements)

References 24 publications

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“…Also, it has been reported that with alkaline treatment, the structure of protein isolates in the rice residue was greatly damaged due to the alkaline denaturation [30]. These studies confirm that alkaline conditions are unfavorable for the stability of ACE-inhibitory activity of JHP.…”

Section: Effect Of Ph On Ace-inhibitory Activity Of Jhpmentioning

confidence: 55%

Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham

Zuo¹,

Zhang²,

Xing³

et al. 2017

JFNR

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Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides extracted from traditional dry-cured Jinhua ham was investigated. The ACE-inhibitory activity was measured after the treatments of heat, NaCl, pH and simulated gastro-intestinal digestion. Peptides possessed an ACE-inhibitory activity of 53.53% at 10 mg/mL and showed a good stability against different heating temperatures (up to 100°C), heating times (up to 60 min) and acid conditions. The NaCl had no significant effects on the ACE-inhibitory activity, while there was a sharp decline under alkaline condition. The ACE-inhibitory activity increased by 4.01% after pepsin treatment and then remained constant after trypsin treatment. The increased ACE-inhibitory activity after pepsin digestion could be explained by the greater exposure of hydrophobic residues. In this study, peptides extracted from Jinhua ham were proved to have ACE-inhibitory activity which showed a good stability against various processing conditions as well as the simulated gastro-intestinal digestion.

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Section: Effect Of Ph On Ace-inhibitory Activity Of Jhpmentioning

confidence: 55%

Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham

Zuo¹,

Zhang²,

Xing³

et al. 2017

JFNR

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“…The protein solution was thoroughly dispersed as described in EAI determination. The foaming capacity was calculated as follows (Hou et al, )

Foaming capacity (() %) = \frac{V_{W} - V_{O}}{V_{normalO}}

where V W is the volume of protein solution after whipping; V O is the volume of solution before whipping.…”

Section: Methodsmentioning

confidence: 99%

“…These techniques focused on alkali concentration and extraction parameters leading to high yield to the neglect of possible nutritional and safety concerns that may arise due to alkali use. The use of alkali in protein extraction may lead to the generation of noxious substances such as lysinoalanine through intermolecular cross‐coupling and rearrangement of proteins (Hou et al, ). Lysinoalanine functions as a bridge between two different sections of a protein chain and then impedes the approach of enzymes consequently leading to decrease in protein digestibility (Boschin, Agostina, Rinaldi, & Arnoldi, ).…”

Section: Introductionmentioning

confidence: 99%

Effect of alkali concentration on functionality, lysinoalanine formation, and structural characteristics of tea residue proteins

Ayim

Alenyorege

et al. 2018

J Food Process Engineering

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The effect of varying sodium hydroxide concentration on functionality, structural characteristics, and the generation of lysinoalanine from tea protein extraction was explored. The results indicated that increasing alkali molarity from 0.0125 to 0.150 M resulted in an increase in protein yield, solubility, foam capacity, and stability up to 0.1 M, which declined further with an increase in the alkali concentration. Surface hydrophobicity, thiol, and disulfide contents reached a maximum at 0.075 M and continued to decline afterward. The effect of alkaline concentration on lysinoalanine (LAL) formation showed an increase from 6.00 ± 0.32 g/kg at 0.1 M to 29.43 ± 1.10 g/kg at 0.125 M followed by a decline to 7.37 ± 0.01 g/kg at 0.15 M. There was a significant (p < .05) reduction in Cys and Lys contents as alkali concentration increased. The use of alkali in extracting protein from tea and other plant sources should be monitored as higher alkali concentration may pose a nutritional concern. Practical applications Extraction of protein from plant sources is most often facilitated by use of alkali. However, the adverse effect of use of alkali is not considered in most cases. The use of sonication, ethanol, and Viscozyme pretreatments coupled with varying alkali concentration was adopted to extract proteins from tea residue and the generation of lysinoalanine, a toxic substance was quantified. The use of alkali at higher concentrations could pose a nutritional concern as it caused an increase in lysinoalanine content. Improved protein yield and purity can be achieved at moderately lower alkali concentrations.

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“…[25][26][27] And the quarternary structure of protein was destroyed, which resulting into a good dissolution characteristic aer adjusting the pH to 7.0. 27,28 In such suspension condition, the surface charge of PPI fractions was negative. And then the addition of calcium ion was a trigger and interference for system charge re-balance and PPI protein was tending to gather together around calcium ion to realize the electric neutrality of whole suspension.…”

Section: Nanoparticle Characterizationmentioning

confidence: 99%

“…With the increase of pH from 8 to 11, PPI was tending to more and more hydration, the interaction between subunits (protein quaternary structure) was gradually broken, and the size of PPI fractions was cut down. 27,28 And nally, the size of PPI nanoparticles was decreased. However, the size was increased again when pH changed to 12.…”

mentioning

confidence: 98%

Synthesis and characterization of calcium-induced peanut protein isolate nanoparticles

et al. 2017

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A convenient and green synthetic route using calcium ion induction was first used to prepare peanut protein isolate (PPI) nanoparticles. Through dynamic light scattering (DLS) and transmission electron microscopy (TEM), the role of each procedure in the formation of nanoparticles was systematically investigated by means of particle size, size distribution, and morphology observation. The size of the obtained nanoparticles ranged from 80 to 140 nm, and they exhibited a uniform size distribution and spherical shape. After dry processing, PPI nanoparticles still display a good state in terms of size and morphology.Stability test results indicated that PPI nanoparticles have good thermal stability, gastrointestinal pH stability, dilution stability and storage stability. In particular, these nanoparticles still have good stability with their concentration diluted to 0.05 mg mL À1 while they can be stored for up to 60 days with particle sizes still below 120 nm at room temperature. All these features endow PPI nanoparticles with great potential in the delivery of bioactive compounds.

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Alkali solution extraction of rice residue protein isolates: Influence of alkali concentration on protein functional, structural properties and lysinoalanine formation

Cited by 185 publications

References 24 publications

Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham

Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham

Effect of alkali concentration on functionality, lysinoalanine formation, and structural characteristics of tea residue proteins

Synthesis and characterization of calcium-induced peanut protein isolate nanoparticles

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