Emulsion stabilization by tomato seed protein isolate: Influence of pH, ionic strength and thermal treatment

Sarkar, Anwesha; Kamaruddin, H.D.; Bentley, Annie; Wang, Shikai

doi:10.1016/j.foodhyd.2016.01.014

Cited by 85 publications

(60 citation statements)

References 38 publications

(51 reference statements)

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“…Tris‐Tricin SDS–PAGE (Figure ) showed that in‐depth digestion took place during the enzymolysis. Main polypeptides bands detected in UTSP were globulin, albumin, prolamin, and glutelin (10–50 kDa) after comparison with literature data available on tomato seed proteins (Sarkar et al, ). These polypeptide bands disappeared almost completely in the antioxidant and ACE inhibitory TSPHs while new polypeptides of lower molecular weights appeared.…”

Section: Resultsmentioning

confidence: 90%

“…Overall, there was an increased solubilization of polypeptides with increasing pH except for the calcium binding TSPH. The isoelectric point of the tomato seed proteins was reported to be around pH 3.5 based on zeta potential and solubility measurements (Sarkar, Kamaruddin, Bentley, & Wang, ). It is therefore not surprising that in this work, the lower solubility was obtained at pH 2–7 for non‐digested proteins (UTSP) while the highest was achieved at pH 10.0 which might explained by greater concentrations of the main polypeptides (globulins) as reported for a study on bean proteins with similar composition of globulins (Fukuda, Prak, Fujioka, Maruyama, & Utsumi, ).…”

Section: Resultsmentioning

confidence: 99%

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Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

et al. 2018

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The objective of this was to determine the impact of enzymatic hydrolysis on the multifunctionality of tomato seed protein hydrolysates (TSPH) and their physicochemical properties. The enzymatic hydrolysis was performed using alcalase and two factors response surface methodology. The best conditions were 131.4 min and 3% enzyme/substrate (E/S) for antioxidant activity; 174.5 min and 2.93% E/S for angiotensin‐converting enzyme (ACE) inhibition; and 66.79 min and 2.27% E/S for the calcium binding. Antioxidant and ACE hydrolysates were characterized by higher solubility, zeta potential, and thermal stability while properties of the calcium binding hydrolysate were only minimally affected by the enzymatic hydrolysis. Gel electrophoresis showed that molecular weights of polypeptides in the calcium binding TSPH were higher compared to those in ACE and antioxidant TSPHs. This was due to the low degree of hydrolysis of the calcium binding hydrolysate. Practical applications Nowadays, different protein sources are used to produce protein hydrolysates containing bioactive peptides that can help alleviate oxidation of foods, oxidative stress, and chronic conditions (e.g., hypertension, diabetes, cardiovascular disorder). Hydrolyzed proteins also have the potential to increase mineral absorption through the formation of mineral‐binding complexes. Biological activities of proteins and peptides from tomato processing byproduct (i.e., pomace) have received until now little attention. The determination of physicochemical properties and biological activities of the hydrolyzed proteins has application in the formulation of value‐added food products for the reduction of oxidative stress and risks of developing chronic diseases. In addition, there will be a reduction of pomace waste generated by the tomato processing industry.

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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

et al. 2018

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“…Steric stabilization, interfacial elasticity, and pH value would also affect emulsion stability of protein. When emulsion pH was far from protein's isoelectric point, high electrostatic repulsion between oil droplets was prone to cause strong emulsion stability (Lam & Nickerson, ; Sarkar, Kamaruddin, Bentley, & Wang, ). Steric stabilization induced by “loops” or “tails” of protein segments may prevent droplets from flocculation and aggregation (Lam & Nickerson, ).…”

Section: Resultsmentioning

confidence: 99%

“…However, R 2 was low with the value of .79332, and many experimental data points deviated from the regression curve. Moreover, as shown in droplets was prone to cause strong emulsion stability (Lam & Nickerson, 2013;Sarkar, Kamaruddin, Bentley, & Wang, 2016). Steric stabilization induced by "loops" or "tails" of protein segments may prevent droplets from flocculation and aggregation (Lam & Nickerson, 2013).…”

Section: Correlation Analysis For Surface Hydrophobicity and Surfacmentioning

confidence: 99%

Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Sha

et al. 2018

J Food Process Preserv

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Dynamic high pressure microfluidization (DHPM) was applied to treat fish gelatin from bighead carp (Hypophthalmichthys nobilis) scale. The effects of various pressures from 40 to 160 MPa on the functional properties and structural characteristics of fish gelatin were evaluated. The results showed that DHPM significantly improved the emulsifying and foaming properties, as well as the in vitro pepsin digestibility. Surface hydrophobicity of treated fish gelatin was considered to be highly correlated to emulsifying activity with R2 of .99933. DHPM could not change gel strength and molecular weight distribution of fish gelatin, but decreased its melting temperature with the increased pressures. Micro‐structural analysis showed that DHPM endowed fish gelatin with polyporous, rough but uncracked microstructure. Practical applications In spite of possessing relatively low melting temperature, fish gelatin is a suitable replacement for mammalian gelatin in low‐temperature stored foods including milk and yogurt. At this time, surface‐active properties including foaming and emulsifying properties are generally the most important factor for ensuring food quality. However, fish gelatin shows relatively weaker surface‐active properties, especially emulsifying/stabilizing function. Our results show DHPM is a physical technology to enhance the surface‐active properties of fish gelatin. DHPM will be promising to promote fish gelatin for its applications in the food industry.

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“…For the products ADP, the dl-a-tocopherol acetate was 0.132% and changed the CaCl 2 for NaCl (0.051%) to help the charge stabilization (Sarkar et al 2016). The emulsions were prepared in a vacuum homogenizer (Ultraturrax T25 -Janke & Kunkel IKA -Labortechnik) for 20 minutes to 24000rpm.…”

Section: Methodsmentioning

confidence: 99%

Calidad de productos deshidratados de manzana adicionados con componentes activos

Cortés

Chiralt

2016

rcia

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RESUMENEl objetivo de la presente investigación fue evaluar los atributos de calidad de manzanas secadas por aire convencional y liofilizadas, previo tratamiento de impregnación (IV) con vitamina E. El proceso de secado por aire convencional (PSAC) se realizó en un secador de bandeja a 40ºC, humedad relativa de 59±7% y velocidad del aire de 0,7 m/s; mientras que, el proceso de liofilización (PL) se realizó a presión de vacío de 1.2 x 10 -3 kPa, temperatura del condensador de -45ºC y temperatura de la bandeja de 25ºC. La cuantificación de vitamina E se realizó por cromatografía de gases con detector de ionización de llama sobre extractos de las muestras en hexano. Las manzanas PSAC y PL presentaron 0,72±0,12 y 1,34±0,14mg dl-α-tocoferol acetato/g; 12,6±1,7 y 7,9±2,0% humedad, respectivamente. Los productos PSAC presentaron pardeamiento, mientras que los productos PL fueron más claros (>L*), verdosos (L*), greenish (

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Emulsion stabilization by tomato seed protein isolate: Influence of pH, ionic strength and thermal treatment

Abstract: This is a repository copy of Emulsion stabilization by tomato seed protein isolate: Influence of pH, ionic strength and thermal treatment.

Cited by 85 publications

References 38 publications

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Calidad de productos deshidratados de manzana adicionados con componentes activos

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