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    NLM-PubMed-Logo  doi: 10.17113/ftb.55.03.17.5200 

Extraction of Proanthocyanidins and Anthocyanins from Grape Skin by Using Ionic Liquids



Natka Ćurkosmall orcid_display_4pp, Marina Tomaševićsmall orcid_display_4pp, Marina Cvjetko Bubalosmall orcid_display_4pp, Leo Gracinsmall orcid_display_4pp, Ivana Radojčić Redovniković*small orcid_display_4pp
and Karin Kovačević Ganićsmall orcid_display_4pp



University of Zagreb, Faculty of Food Technology and Biotechnology, Pierottijeva 6, HR-10000 Zagreb, Croatia



Article history:
Received: February 6, 2017
Accepted: April 24, 2017
cc


Key words:
anthocyanins, grape skin, HPLC, ionic liquids, proanthocyanidins



Summary:
In this study, eight different types of imidazolium-based ionic liquids (ILs) were applied as new solvents in the extraction of flavonoids from grape skin, and compared to the conventional organic solvent extraction that was not reported earlier. The structure of anions, cations and concentration of ILs significantly affected extraction yields. The highest mass fractions of proanthocyanidins and anthocyanins were obtained with 2.5 mol/L of 1-butyl-3-methylimidazolium bromide [C4mim][Br] and 2.5 mol/L of 1-ethyl-3-methylimidazolium bromide [C2mim][Br], respectively. The studied ILs provided an excellent preliminary result in the extraction of anthocyanins. Significantly higher mass fractions of total and all free anthocyanins were extracted with 2.5 mol/L of [C2mim][Br] and 2.5 mol/L of 1-methylimidazolium hydrogen sulfate [mim][HSO4] than with conventional solvent with the exception of anthocyanin-3-O-acetylmonoglucosides in the latter. On the other hand, 2.5 mol/L of [C4mim][Br] and 2.5 mol/L of 1-(4-sulfobutyl)-3-methylimidazolium hydrogen sulfate [sC4mim][HSO4] showed significantly higher selectivity towards anthocyanin-3-O-acetylmonoglucosides and anthocyanin-3-(6-O-p-coumaroyl)monoglucosides.



*Corresponding author:  tel3  +385 1 4605 015
                                            email3  iradojci@pbf.hr


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   NLM-PubMed-Logo  doi: 10.17113/ftb.55.03.17.5061 

Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate Obtained from Industrial Sunflower Meal



Petya Ivanova1small orcid_display_4pp, Vesela I. Chalova1*small orcid_display_4pp, Hristo Kalaydzhiev1small orcid_display_4pp, Mariana Perifanova-Nemska2small orcid_display_4pp, Turid Rustad3small orcid_display_4pp
and Lidia Koleva1small orcid_display_4pp



1University of Food Technologies, Department of Biochemistry and Molecular Biology, 26 Maritsa Bulv., BG-4002 Plovdiv,
  Bulgaria
2University of Food Technologies, Department of Technology of Tobacco, Sugar, Vegetable and Essential Oils, 26 Maritsa
  Bulv., BG-4002 Plovdiv, Bulgaria
3Norwegian University of Science and Technology, Department of Biotechnology and Food Science, Sem Salandsvei 6/8,
  NO-7491 Trondheim, Norway



Article history:
Received: November 15, 2016
Accepted: May 4, 2017
cc


Key words:
industrial sunflower meal, pepsin, protein hydrolysates, transglutaminase modification, functional properties



Summary:
The utilization of industrial sunflower meal to produce protein-rich products for the food industry is an alternative approach for better and more efficient use of this agricultural by-product. Sunflower meal proteins possess specific functional properties, which however need improvement to broaden their potential as supplements for delivering high-quality products for human nutrition. The aim of the study is to evaluate the combined influence of low-degree pepsin hydrolysis and transglutaminase (TG) modification on industrial sunflower meal protein isolate functionality at pH=2 to 10. Three TG-modified pepsin hydrolysates with the degree of hydrolysis of 0.48, 0.71 and 1.72 % were produced and named TG-PH1, TG-PH2 and TG-PH3, respectively. All three TG-modified pepsin hydrolysates exhibited improved solubility at pH between 3.5 and 5.5 as the highest was observed of TG-PH3 at protein isoelectric point (pI=4.5). Sunflower meal protein isolate and TG-modified sunflower meal protein isolate had greater solubility than the three TG-modified hydrolysates at pH<3 and >7. Significant improvement of foam making capacity (p<0.05) was achieved with all three TG-modified pepsin hydrolysates in the entire pH area studied. Pepsin hydrolysis of the protein isolate with the three degrees of hydrolysis did not improve foam stability. Improved thermal stability was observed with TG-PH3 up to 80 °C compared to the protein isolate (pH=7). At 90 °C, TG modification of the protein isolate alone resulted in the highest thermal stability. Pepsin hydrolysis followed by a treatment with TG could be used to produce sunflower protein isolates with improved solubility, foam making capacity and thermal stability for use in the food industry.



*Corresponding author:  tel3  +359 32 603 855
                                           fax2  +359 32 644 102
                                            email3  veselachalova@gmail.com


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   NLM-PubMed-Logo  doi: 10.17113/ftb.55.03.17.4873 

The Effect of High Pressure and Subzero Temperature on Gelation of Washed Cod and Salmon Meat



Edyta Malinowska-Panczyk*small orcid_display_4pp and Ilona Kolodziejska



Department of Food Chemistry, Technology and Biotechnology, Chemical Faculty, Gdansk University of Technology, G.
Narutowicza 11/12, PL-80-233 Gdansk, Poland



Article history:
Received: July 6, 2016
Accepted: June 27, 2017
cc


Key words:
high pressure processing, subzero temperature, washed cod and salmon meat, gelation, properties of myofibrillar proteins



Summary:
The objective of the present work is to examine the influence of pressure up to 193 MPa at subzero temperature (without freezing of water) on myofibrillar proteins of salmon and cod meat and on the properties of gels obtained from washed mince of these fish. The solubility of proteins from myofibrils of cod and salmon meat suspended in 100 mM KCl solution increased after treating the samples with pressure above 60 MPa. The results of SDS-PAGE analysis showed that under these conditions two myosin light chains, tropomyosin and troponin T were released from myofibrils. The solubility of proteins in 0.9 M NaCl solution of washed fish meat after pressure treatment at 60 MPa and –5 °C decreased to about 80–90 % and at 193 MPa and –20 °C to 60 %. Pressurization of cod meat decreased only slightly the solubility of proteins in SDS and urea solution and the solubility of salmon meat was similar to that in the unpressurized sample. There were no differences in the electrophoretic pattern of proteins from untreated and pressurized cod and salmon meat in the range of 60 to 193 MPa and –5 to –20 °C. The pressure treatment of washed salmon and cod meat at a temperature below 0 °C induced gelation; on the other hand, hardness of gels was lower by 28 and 26 %, respectively, than that of gels formed by heating. The salmon and cod gels pressurized at 193 MPa and –20 °C and then heated were much harder than only pressurized or heated gels.


*Corresponding author:  tel3  +48 58 347 2656
                                           fax2  +48 58 347 2694  
                                                  email3  edyta.malinowska-panczyk@pg.gda

 


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   NLM-PubMed-Logo  doi: 10.17113/ftb.55.03.17.4981 

Solid-State Fermentation Reduces Phytic Acid Level, Improves the Profile of Myo-Inositol Phosphates and Enhances the Availability of Selected Minerals in Flaxseed Oil Cake



Robert Duliński1*small orcid_display_4pp, Bożena Stodolak1small orcid_display_4pp, Łukasz Byczyński1small orcid_display_4pp, Aleksander Poreda2small orcid_display_4pp, Anna Starzyńska-
-Janiszewska1small orcid_display_4pp and Krzysztof Żyła1small orcid_display_4pp



1Department of Food Biotechnology, Faculty of Food Technology, University of Agriculture in Krakow, ul. Balicka 122,
  PL-30-149 Kraków, Poland
2Department of Fermentation Technology and Technical Microbiology, Faculty of Food Technology, University of
  Agriculture in Krakow, ul. Balicka 122, PL-30-149 Kraków, Poland



Article history:
Received: September 8, 2016
Accepted: May 4, 2017
cc



Key words:
flaxseed oil cake, solid-state fermentation, phytates, myo-inositol phosphates, mineral availability



Summary:
Flaxseed oil cake was subjected to fermentation with Rhizopus oligosporus (DSM 1964 and ATCC 64063), and the phytate (InsP6) content, myo-inositol phosphate profile and in vitro bioavailability of essential minerals were studied. Flaxseed oil cake had a phytate mass fraction of 13.9 mg/g. A 96-hour fermentation of flaxseed oil cake by R. oligosporus DSM 1964 and R. oligosporus ATCC 64063 decreased the InsP6 content by 48 and 33 %, respectively. The strains had different phytate-degrading activities: fermentation of flaxseed oil cake with R. oligosporus DSM 1964 was more advantageous, yielding InsP3-5 as a predominating myo-inositol compound, while fermentation with R. oligosporus ATCC 64603 produced predominantly InsP5-6. Solid-state fermentation of flaxseed oil cake enhanced in vitro bioavailability of calcium by 14, magnesium by 3.3 and phosphorus by 2–4 %.



*Corresponding author:  email3  r.dulinski@ur.krakow.pl


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   NLM-PubMed-Logo  doi: 10.17113/ftb.55.03.17.5001 

Effect of Amidated Low-Methoxyl Pectin on Physicochemical Characteristics of Jumbo Squid (Dosidicus gigas) Mantle Muscle Gels



Juan C. Ramirez-Suarez1*small orcid_display_4pp, Andrés Álvarez-Armenta1small orcid_display_4pp, Guillermina García-Sánchez1small orcid_display_4pp, Ramón
Pacheco-Aguilar1small orcid_display_4pp, Susana M. Scheuren-Acevedo1small orcid_display_4pp, Miguel A. Mazorra-Manzano2small orcid_display_4pp and Agustín
Rascón-Chu3small orcid_display_4pp


1Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6,
  83304 Hermosillo, Sonora, Mexico
2Dairy Products Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304
  Hermosillo, Sonora, Mexico
3Plants and Fungi Biotechnology Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria
  Km. 0.6, 83304 Hermosillo, Sonora, Mexico



Article history:
Received: September 29, 2016
Accepted: May 23. 2017
cc


Key words:
jumbo squid, amidated low-methoxyl pectin, gelling, water retention



Summary:
Jumbo squid (Dosidicus gigas) muscle proteins show low functionality with limited use in gel products. This work aims to assess the influence of adding the natural and commercially available fibre, amidated low-methoxyl pectin (at 0.5, 1.0, 1.5, 2.0 and 3.0 %), on the physicochemical and functional characteristics of jumbo squid (Dosidicus gigas) mantle muscle gels. The addition of 0.5 % fibre showed an immediate effect on the gel texture profile analysis, improving hardness (p<0.05) from (3.4±0.7) N of the control (no added fibre) to (5.2±0.9) N, and increasing elasticity (p<0.05). Shear force was significant only at 3.0 % fibre addition. Water holding capacity also improved (p<0.05) with fibre addition (from 75 % in the control to 90–95 % after the treatments). Whiteness was affected (p<0.05) when 3.0 % fibre was added. Differential scanning calorimetry showed two endothermic transition peaks in the gels. The second peak (actin) increased (p<0.05) by 1–2 °C with fibre addition. Therefore, the present study demonstrates that amidated low-methoxyl pectin (0.5–3.0 %) is an excellent ingredient to improve jumbo squid mantle muscle protein functionality, increasing the gel texture and water retention characteristics.



*Corresponding author:  tel3  +52 662 289 2400 ext. 368
                                           fax2  +52 662 280 0421
                                            email3  jcramirez@ciad.mx

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