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Journal ArticleDOI

Ultrasonic effect on physicochemical and functional properties of α -lactalbumin

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TLDR
In this article, the effect of ultrasound and sonication on α-lactalbumin (α-LA) with a view to improving its physicochemical and functional properties was examined.
Abstract
Ultrasound is the sound whose frequency is too high for humans to hear which is within the frequency range of 20 Hz–20 kHz, and the frequency of ultrasound is above 20 kHz. The aim of this study was to observe the effect of ultrasound and sonication on α-lactalbumin (α-LA) with a view to improving its physicochemical and functional properties. In this work both low-intensity ultrasound (500 kHz bath) and the high-intensity ultrasound (20 kHz probe and 40 kHz bath) were used. Ten per cent wt (g g−1 dry matter) protein model suspensions of α-lactalbumin (α-LA) were treated with ultrasound probe (20 kHz for 15 and 30 min) and ultrasound baths (40 kHz and 500 kHz for 15 and 30 min). Changes in pH values, electrical conductivity, solubility measurements, foaming properties, as well as rheological and freezing-thawing properties have been examined. The protein fractions of α-lactalbumin were analyzed before and after ultrasound treatment by SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis). The result showed that pH did not change significantly upon ultrasound however conductivities increased significantly after 20 kHz sonication. Electrical conductivity decreased significantly for ultrasound treatments in baths at 40 kHz and 500 kHz for all samples. Solubility increased significantly for all samples at 20 kHz. Foam capacities and foam stabilities were improved after ultrasound treatments for both 20 kHz and 40 kHz treatments. Foaming properties were not improved for protein model suspensions for 500 kHz treatments. The molecular weight of the protein decreased significantly after ultrasound treatments both using a 20 kHz probe and 40 kHz bath. The flow behaviour of α-lactalbumin was observed to be shear-thickening after all treatments. Apparent viscosity data calculated with power law equation (R2 = 0.983–0.999) have not been changed significantly after all treatments. A remarkable decrease of initial freezing point was obtained after 20 kHz treatments.

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Citations
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Comparative study of high intensity ultrasound effects on food proteins functionality

TL;DR: In this paper, the authors explored the impact of high intensity ultrasound (HIUS) on the functionality of some of the most used food proteins at the industrial level: whey protein concentrate (WPC), soy protein isolate (500E), and egg white protein (EW).
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Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel.

TL;DR: Low field NMR data showed that bound water had lower water mobility and was more closely associated with proteins in HIU treated MP gel, while the proportions of immobilized water and free water had their maximum and minimum value, respectively, at 600W.
Journal ArticleDOI

Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments.

TL;DR: High intensity ultrasonic pre-treatments of soybean protein isolate (SPI) improved the water holding capacity (WHC), gel strength and gel firmness (final elastic moduli) of glucono-δ-lactone induced SPI gels (GISG).
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High intensity ultrasound treatment of protein isolate extracted from dephenolized sunflower meal: Effect on physicochemical and functional properties

TL;DR: Solubility, emulsifying capacity, emulsion stability, foaming capacity, foam stability and oil binding capacity were improved significantly, while as, water binding capacity was decreased.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
PatentDOI

Measurement of protein using bicinchoninic acid

TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
Journal ArticleDOI

Functional properties of proteins in foods: A survey

TL;DR: In this paper, the major functional properties of food proteins, e.g., solubility, binding properties, surfactant properties, viscogenic texturizing characteristics, etc.
Journal ArticleDOI

Applications and opportunities for ultrasound assisted extraction in the food industry-a review

TL;DR: In this paper, the use of ultrasonic assisted extraction (UAE) for food and allied industries is discussed, including the potential for modification of plant cell material to provide improved bioavailability of micro-nutrients while retaining the natural-like quality.
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