Solubility properties of barley flour, protein isolates and hydrolysates

Yalçın, Erkan; Çelik, Süeda

doi:10.1016/j.foodchem.2007.03.029

Cited by 52 publications

(22 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Several researchers have shown that most vegetable proteins have the lowest protein solubility at their isoelectric point and then increased for basic pH values, this behaviours is similar to that of many other vegetable proteins reported earlier (Yalçin & Celik, 2007).…”

Section: Solubilitysupporting

confidence: 81%

“…1, the hydrolysis proceeded at a low initially rate with DH reaching only 2.65 AE 0.04% after 2 h. According to Yalçin and Celik (2007), this slower initial hydrolysis for BSG protein can be attributed to its greater content of inter-chain disulfite bonds making it more resistant to proteases. After this initial induction period, the hydrolysis BSG protein likely unfolds and becomes susceptible to the action of proteases, leading to an increased hydrolysis rate.…”

Section: Hydrolysates Preparationmentioning

confidence: 97%

“…Researchers have studied the limited hydrolysis by using various proteases in order to increase the solubility properties of the plant proteins (Yalçin & Celik, 2007).…”

Section: Solubilitymentioning

confidence: 99%

See 2 more Smart Citations

Improvement of functional and antimicrobial properties of brewery byproduct hydrolysed enzymatically

Kotlar

Ponce

Roura

2013

LWT - Food Science and Technology

View full text Add to dashboard Cite

Section: Solubilitysupporting

confidence: 81%

Section: Hydrolysates Preparationmentioning

confidence: 97%

See 1 more Smart Citation

Improvement of functional and antimicrobial properties of brewery byproduct hydrolysed enzymatically

Kotlar

Ponce

Roura

2013

LWT - Food Science and Technology

View full text Add to dashboard Cite

“…Although chemical treatments are less expensive, more insoluble collagen is produced. Therefore, enzymatic hydrolysis has been used as a strategy to improve protein solubility, by disrupting the native interactions of the protein and exposing the hydrophilic amino acids and releasing protein segments of lower molecular weight, thus increasing its solubility (Yalçın & Çelik, 2007). Further enzymatic hydrolysis can expose functional groups that may have antioxidant, antimicrobial, antiproliferative or antimutagenic activity with a beneficial impact on health (Han, Uzawa, Moriyama, & Kawamura, 2011).…”

Section: Introductionmentioning

confidence: 99%

Collagen from jumbo squid fin: extracting conditions and influence of the protease system on collagen hydrolysate antioxidant activity

Cuevas-Acuña

Robles-Sánchez

Torres‐Arreola

et al. 2015

CyTA - Journal of Food

View full text Add to dashboard Cite

Collagen from jumbo squid fin: extracting conditions and influence of the protease system on collagen hydrolysate antioxidant activity Colágeno de aletas de calamar gigante: condiciones de extracción y efecto del sistema proteolítico en la actividad antioxidante de sus hidrolizados The optimal alkaline and acid conditions for insoluble collagen extraction from jumbo squid fin (JSF) were established by factorial analysis. Dependent variable: protein concentration; independent variables: NaOH and HCl concentrations. The antioxidant properties of JSF collagen hydrolysates obtained by two protease systems were studied. Moreover, jumbo squid skin (JSS) collagen was obtained and hydrolysated under optimal conditions. The optimal extraction condition was 0.5 M NaOH followed by 0.2 M HCl. Collagen α-chains were detected in both JSF and JSS. Collagen β-component was detected only in JSS. JSS collagen showed higher levels of polar and hydrophobic amino acids. The JSF hydrolysates produced by subtilisin showed a lower degree of hydrolysis and higher antioxidant activity (2,2-diphenyl-1-picrylhydrazyl (DPPH), Trolox equivalent antioxidant capacity (TEAC), and oxygen radical absorbance capacity-fluorescein (ORAC FL )) than those produced by a mixture of trypsin, chymotrypsin, and peptidase. The JSS hydrolysates showed a higher antioxidant capacity. We have thus established a suitable process to improve the utility of JSF.Keywords: fin collagen; extraction conditions; protease system; hydrolysate; antioxidant activity La mejores condiciones para la extracción del colágeno insoluble de las aletas del calmar gigante (JSF) fueron establecidas aplicando un diseño factorial. Variable dependiente: concentración de proteína; variables independientes: concentraciones de NaOH y HCl. Se comparó la actividad antioxidante de hidrolizados del colágeno de JSF, obtenidos mediante dos sistemas proteolíticos. Además, usando las mejores condiciones se extrajo el colágeno de la piel del calamar (JSS) e hidrolizó. Las mejores condiciones de extracción fueron: NaOH 0.5 M y HCl 0.2 M. Las bandas α se observaron en ambos colágenos. El β-componente de colágeno solo se detectó en JSS. JSS mostró mayor contenido de aminoácidos polares e hidrofóbicos. Los hidrolizados de JSF producidos por subtisilina presentaron menor grado de hidrólisis, la más alta actividad antioxidante (DPPH, TEAC, ORAC FL ) que los obtenidos por una mezcla de tripsina, quimotripsina y peptidasas. Los hidrolizados del JSS mostrarón la mayor actividad antioxidante. Se estableció un proceso para un mejor aprovechamiento de JSF.

show abstract

“…The classical Osborn method has been used to isolate fractions from barley grains (Kapp and Bamforth 2002;Yalçin and Çelik 2007;Yalçin et al 2008). Recently, it is more common to use a detergent (e.g., SDS or a chaotropic agent such as urea), often in the presence of a reducing agent (Shewry et al 1978;Linko et al 1989;Mohamed et al 2007).…”

mentioning

confidence: 99%

Functionality of Barley Proteins Extracted and Fractionated by Alkaline and Alcohol Methods

et al. 2010

View full text Add to dashboard Cite

Cereal Chem. 87(6):597-606This research optimized the extraction of different protein fractions from barley grains and assessed the physicochemical properties of the fractions obtained. Pearling was first used to remove the grain's outer layers (mainly bran and germ) so that the barley cytoplasmic proteins (albumin and globulin) would be enriched in the pearling flour (PF), while endosperm proteins (hordein and glutelin) would be enriched in the pearled grain flour (PGF). Salt, alcohol, and alkaline solutions were then used to extract different barley protein fractions from PF and PGF. The effects of extraction solvent type, pH, temperature, and extraction time on protein content and extraction efficiency were studied. Aqueous ethanol (55%, v/v) efficiently extracted barley hordein from PGF at 60°C, whereas pH 11.5 alkaline solution was the most efficient for extracting both cytoplasmic and endosperm proteins from barley PF and PGF at 23°C. Subunit molecular weight, amino acid composition, and the functional properties of each isolated barley protein fraction were investigated. Barley glutelin demonstrated superior oil-binding property and emulsifying stability, whereas barley hordein exhibited good foaming capacity.

show abstract

Solubility properties of barley flour, protein isolates and hydrolysates

Cited by 52 publications

References 31 publications

Improvement of functional and antimicrobial properties of brewery byproduct hydrolysed enzymatically

Improvement of functional and antimicrobial properties of brewery byproduct hydrolysed enzymatically

Collagen from jumbo squid fin: extracting conditions and influence of the protease system on collagen hydrolysate antioxidant activity

Functionality of Barley Proteins Extracted and Fractionated by Alkaline and Alcohol Methods

Contact Info

Product

Resources

About