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New biopolymers by cross-linking whey protein isolate and soybean 11S globulin: Preparation and properties

Başlık çevirisi mevcut değil.

  1. Tez No: 400655
  2. Yazar: METİN YILDIRIM
  3. Danışmanlar: DR. NAVAM S. HETTIARACHCHY
  4. Tez Türü: Doktora
  5. Konular: Besin Hijyeni ve Teknolojisi, Beslenme ve Diyetetik, Gıda Mühendisliği, Food Hygiene and Technology, Nutrition and Dietetics, Food Engineering
  6. Anahtar Kelimeler: Belirtilmemiş.
  7. Yıl: 1998
  8. Dil: İngilizce
  9. Üniversite: University of Arkansas
  10. Enstitü: Yurtdışı Enstitü
  11. Ana Bilim Dalı: Belirtilmemiş.
  12. Bilim Dalı: Belirtilmemiş.
  13. Sayfa Sayısı: 126

Özet

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Özet (Çeviri)

Biopolymers were prepared by cross-linking whey protein isolate (WPI) and soybean US globulin (US) using transglutaminase (TG). Solubility, emulsification, hydrophobicity and foaming properties of the biopolymers were examined. Differential scanning calorimetry (DSC) was used to determine thermal properties of proteins and biopolymers. Partial purification of biopolymers was carried out using Sepharose 4B column. The extent of polymerization was determined by electrophoresis and HPLC. Ultraviolet (UV) and fluorescence spectra were used to analyze structural changes of biopolymers. SDS-PAGE showed bands corresponding to high-molecular-weight components (MW > 200 kDa). Molecular weight distribution of purified biopolymers in non-denaturing and non-reducing conditions ranged from 670 kDa -to 20,000 kDa which was the excluding limit of the Sepharose 4B column. Ultra violet and fluorescence spectra showed that cross-linking of US and WPI did not cause any significant structural changes. Biopolymer solubility was > 90% at pH 3.0 and below, and at pH 7.0 and above. Emulsifying properties of biopolymers were lower than those of WPI. The foaming capacity of the biopolymers (24 mL) and WPI/11S mixture (23 mL) were similar to that of egg albumin (20 mL). The foaming stability of the biopolymers (122 min) was higher than that of WPI/1 IS mixture (36 min), and was similar to that of egg albumin (132 min). Heterogeneity of biopolymers was determined by cross-linking acetylated-HS acidic, subunits (Ac-ilS) of soy protein with aTactalbumin and Mactoglobulin. HPLC data demonstrated the absence of biopolymers from Ac-llS, acetylated a-lactalburnin and acetylated B-lactogtobulin when each was incubated separately with transglutaminase (TG). However, Ac-llS formed biopolymers with ct-lactalbumin and B-lactoglobulin when TG was added. TG catalyzed the formation of heterologous and homologous biopolymers from WPI and US. Cross-linking WPI and US provided biopolymers with improved heat stability which may be useful to provide functionality to food products. Protein films were produced from WPI, 11S and a mixture of these two proteins (1:1, wt/wt) using TG catalysis. Solubility of TG cross-linked films was lower than that of control films at pH 3,0, 4.0, 6.0 and 8.0. Solubility of control films in 6.6 M urea and in 10% ST>S was higher than that of TG cross-linked films. Hydrolysis of control and TG cross-linked films by trypsin and a-chymotrypsin was similar after 24 hr incubation. Mean thickness of films ranged from 69 to 77 /tm. There were no significant differences among film thicknesses. The average tensile strength values of TG cross-linked films were two times greater than those of the homologous controls.

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