I.

Journal of Functional Foods

Volume 9, July 2014, Pages 1017

High quality fish protein hydrolysates prepared from

by-product material with Fucus vesiculosus extract

Sigrun M. Halldorsdottira, b, , ,
Holmfridur Sveinsdottirc,
Agusta Gudmundsdottirb,
Gudjon Thorkelssona, b,
Hordur G. Kristinssona, d
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doi:10.1016/j.jff.2014.04.009
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Highlights

Oxidation took place during freeze drying of hydrolyzed cod bone mince

Fucus vesiculosus extract protected the fish protein during freeze drying

Fucus vesiculosus extract

hydrolysates

contributed

to

better

tasting

fish

protein

Generally cod bone mince hydrolysates exhibited strong antioxidant activity

Abstract
Value added products such as fish protein hydrolysates (FPH) can be
produced from fish by-products. Lipid oxidation and bad taste are the major
challenge in the commercialization of bioactive FPH. The aim of this research
was to study the production of high quality FPH from fish by-products
prepared by enzymatic hydrolysis using a natural antioxidant extracted from
the Icelandic brown algae Fucus vesiculosus (Fv). FPH were produced from
cod waste material; i.e. cod bone mince, in the absence and presence of
an Fvextract (Fv-e). Oxidation during the FPH production was evaluated (lipid
hydroperoxides and thiobarbituric acid reactive substances). The FPH were
sensory analyzed (generic descriptive analysis) and in vitroantioxidant
activity was evaluated. Results show that Fv-e contributed to better tasting
FPH with regard to bitter, soap, fish oil and rancidity taste. Results from the
oxidation and antioxidant activity assays indicated a protecting effect of Fve during processing.

Keywords

Fish protein hydrolysates;

Fucus vesiculosus extract;
Enzyme hydrolysis;
Lipid oxidation;
Antioxidant activity;
Sensory analysis
Corresponding author. Tel.: +354 4225000/+354 8651704; fax: +354
4225001.
Copyright 2014 Elsevier Ltd. All rights reserved.

II.

Ultrasonics Sonochemistry
Available online 16 January 2015
In Press, Corrected Proof Note to users

Modification of foaming properties of soy protein

isolate by high ultrasound intensity: Particle size
effect

Roco Morales,
Karina D. Martnez, ,
Vctor M. Pizones Ruiz-Henestrosa,
Ana M.R. Pilosof
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doi:10.1016/j.ultsonch.2015.01.011
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Highlights

High intensity ultrasound (HIUS) functionality effects on soy protein were

studied.

Protein particles size, foaming and interfacial measurement were made.

HIUS improved
temperature.

the

foaming

capacity

with

synergistic

result

The foaming capacity and the particle size were correlated.

The invariable stability of foams was related to interfacial studies.

Abstract

with

The effect of high intensity ultrasound (HIUS) may produce structural

modifications on proteins through a friendly environmental process. Thus,
it can be possible to obtain aggregates with a determined particle size, and
altering a defined functional property at the same time.
The objective of this work was to explore the impact of HIUS on the
functionality of a denatured soy protein isolate (SPI) on foaming and
interfacial properties. SPI solutions at pH 6.9 were treated with HIUS for
20 min, in an ultrasonic processor at room temperature, at 75, 80 and
85 C. The operating conditions were: 20 kHz, 4.27 0.71 W and 20% of
amplitude. It was determined the size of the protein particles, before and
after the HIUS treatment, by dynamic light scattering. It was also analyzed
the interfacial behavior of the different systems as well as their foaming
properties, by applying the whipping method.
The HIUS treatment and HIUS with temperature improved the foaming
capacity by alteration of particle size whereas stability was not modified
significantly. The temperature of HIUS treatment (80 and 85 C) showed a
synergistic effect on foaming capacity. It was found that the reduction of
particle size was related to the increase of foaming capacity of SPI. On the
other hand, the invariable elasticity of the interfacial films could explain
the stability of foams over time.

Keywords

Soy protein isolate;

Foaming properties;
Interfacial properties;
Ultrasound
Corresponding author. Tel.: +54 1145763377.
Copyright 2015 Elsevier B.V. All rights reserved.
Note to users: Corrected proofs are Articles in Press that contain the authors' corrections.
Final citation details, e.g., volume and/or issue number, publication year and page numbers,
still need to be added and the text might change before final publication.
Although corrected proofs do not have all bibliographic details available yet, they can already
be cited using the year of online publication and the DOI , as follows: author(s), article title,
Publication (year), DOI. Please consult the journal's reference style for the exact appearance
of these elements, abbreviation of journal names and use of punctuation.
When the final article is assigned to an volumes/issues of the Publication, the Article in Press
version will be removed and the final version will appear in the associated published
volumes/issues of the Publication. The date the article was first made available online will be
carried over.

II.

Food Hydrocolloids
Volume 39, August 2014, Pages 301318

Review

Soy proteins: A review on composition, aggregation

and emulsification

K. Nishinaria, , ,
Y. Fanga, , ,
S. Guob,
G.O. Phillipsa
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doi:10.1016/j.foodhyd.2014.01.013
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Highlights

Factors influencing the gelation of soy protein are described.

Factors influencing emulsification using soy protein are described.

How to enhance the gelling or emulsification are described.

Examples of application are described.

Abstract
Composition of soybean proteins is briefly described. Gels and gelling
processes of soybean proteins and other functionalities such as colloidal
properties and emulsifying properties are described. The effects of
temperature, pH, ionic strength, processing conditions such as high pressure,
ultrasonic treatment, utilisation of enzyme, chemical modification are also
described since they have been found useful to improve the processing and
final product.

Graphical abstract

Keywords

Soy;
Protein;
Gel;
Emulsion;
Process
Corresponding authors. Tel./fax: +86 (0)27 88015996.
Copyright 2014 Elsevier Ltd. All rights reserved.

IV.

Food Hydrocolloids
Volume 43, January 2015, Pages 465472

Understanding the differences in gelling properties

between lupin protein isolate and soy protein isolate

J.A.M. Berghout,
R.M. Boom,
A.J. van der Goot,
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doi:10.1016/j.foodhyd.2014.07.003
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Highlights

Lupin protein isolate forms weaker heat-induced gels than soy protein
isolate.

Lupin protein isolate and soy protein isolate form particle gels.

Lupin protein particles are heat stable.

The sulfhydryl reactivity of lupin protein isolate increases upon heating.


The concentration of free SH groups on soluble proteins is too low for strong
gels.

Abstract
The gelling properties of lupin protein isolate (LPI) were compared with
those of soy protein isolate (SPI). It was found that LPI behaves
fundamentally different than SPI, evidenced by the formation of weaker
and deformable gels. Further investigation shows that both protein isolates
can be considered particle gels and that LPI particles do not swell as much
as SPI particles inside the network. Besides, heating hardly affects LPI
particles while SPI particles show additional swelling. To explain the
differences, the sulfhydryl reactivity of LPI was tested. The amount of free
sulfhydryl groups on LPI was higher than the amount of free sulfhydryl
groups on SPI. Upon heating the amount of free sulfhydryl groups on LPI
increases. We hypothesize that the compact, heat stable structure of the
protein particles suppresses the intermolecular bonding through disulphide
bridge formation and favours intramolecular crosslinking. The small
sulphur-rich proteins that are not incorporated within the particles but are
present in the surrounding solution cannot strengthen the particle network,
due to their low concentration. LPI did not form gels of similar consistency
as SPI and may therefore be less useful for solid food products. The
thermal stability of LPI could offer opportunities for high-protein foods that
require low viscosity after heating.

Graphical abstract

Keywords

Gels;
Lupin protein isolate;
Soy protein isolate;
Rheology;
Sulfhydryl reactivity

Corresponding author. Tel.: +31 317 480852.

Copyright 2014 Elsevier Ltd. All rights reserved.

V.

Journal of Applied Animal Research

Volume 38, Issue 1, 2010

Seleccionar idioma

Translator disclai
mer

Determination of Serum Protein Concentrations in the Arabian Oryx

(Oryx leucoryx) Using Agarose Gel Electrophoresis
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DOI:
10.1080/09712119.2010.9707174
Mansour F. Husseina, H. E. Mohammeda & A. Gar-Elnabia
pages 143-144
Publishing models and article dates explained

Received: 31 Dec 2009

Accepted: 24 Mar 2010

Published online: 14 Nov 2011

Article Views: 12

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Abstract
Hussein, M.F., Mohammed, H.E. and Gar-Elnabi, A. 2010. Determination of serum protein concentrations in the
Arabian oryx (Oryx leucoryx) using agarose gel electrophoresis. J. Appl. Anim. Res., 38: 143144.

Serum proteins of the Arabian oryx (Oryx leucoryx) were quantified in 19 healthy male and female oryxes,
using agarose gel electrophoresis. The mean protein concentrations were as follows: total protein 83.589.55
g/l; albumin 43.449.06 g/l; -globulin 9.303.01 g/l; -globulin 12.306.58 g/l and -globulin 18.246.09
g/l indicating a wide variation in all parameters. No significant differences were found between male and female
oryxes in any of these proteins. This baseline information will be useful for researchers and clinicians.

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Keywords

Arabian oryx,

Oryx leucoryx ,

serum proteins,

electrophoresis
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