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Differential scanning calorimetry (DSC) study of cryoprotective effect of different modified starches on chicken myofibrillar proteins


Kovačević, Dragan; Mastanjević, Krešimir; Šubarić, Drago; Babić, Jurislav
Differential scanning calorimetry (DSC) study of cryoprotective effect of different modified starches on chicken myofibrillar proteins // Proceedings of XIV International Symposium Feed Technology and XII International Symposium NODA 2010 / Jovanka Lević (ur.).
Novi Sad: Institute of Food Technology, 2010. str. 23-29 (predavanje, međunarodna recenzija, cjeloviti rad (in extenso), znanstveni)


Naslov
Differential scanning calorimetry (DSC) study of cryoprotective effect of different modified starches on chicken myofibrillar proteins

Autori
Kovačević, Dragan ; Mastanjević, Krešimir ; Šubarić, Drago ; Babić, Jurislav

Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni

Izvornik
Proceedings of XIV International Symposium Feed Technology and XII International Symposium NODA 2010 / Jovanka Lević - Novi Sad : Institute of Food Technology, 2010, 23-29

ISBN
978-86-7994-018-6

Skup
XIV International Symposium Feed Technology and XII International Symposium NODA 2010

Mjesto i datum
Novi Sad, Srbija, 19-21. 10. 2010.

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Cryoprotection; chicken myofibrillar proteins; DSC; modified starch

Sažetak
Differential scanning calorimetry (DSC) was used to study cryoprotective effects of three different modified starches on chicken myofibrillar proteins. Chicken myofibrillar proteins were prepared from broiler, mixed with tapioca modified starch (MTS1) (w = 5 and 10%), tapioca modified starch (MTS2) (w = 5 and 10%) and barley modified starch (MBS) (w = 5 and 10%), quickly frozen and stored for 90 days on -30 °C. Onset temperature of transition (To), peak thermal transition (Tp), and endset temperature of transition (Te), and denaturation enthalpy (ΔH) were evaluated. Peak (Tp) thermal transition temperatures of chicken myosin showed highest shift to higher values in samples mixed with MBS (w = 5 and 10%). Denaturation enthalpies (ΔH) of chicken myofibrillar proteins showed increase with incense of mass fraction of MBS and decrease with the increase of mass fractions of MTS1 and MTS2. Since the value of denaturation enthalpy is directly related to amount of native proteins, higher values of ΔH indicates higher cryoprotective effects of MBS.

Izvorni jezik
Engleski

Znanstvena područja
Prehrambena tehnologija



POVEZANOST RADA


Projekt / tema
113-1130473-0571 - Razvoj novih modificiranih škrobova i primjena u prehrambenoj industriji (Drago Šubarić, )

Ustanove
Prehrambeno-tehnološki fakultet, Osijek