کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10974288 | 1108024 | 2015 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Solubilization of rehydrated frozen highly concentrated micellar casein for use in liquid food applications
ترجمه فارسی عنوان
جداسازی کازئین میکولر منجمد برای استفاده در برنامه های کاربردی مواد غذایی مایع
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کلمات کلیدی
انحلال پذیری، کازئین میسلر، میکروفیلتراسیون،
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم دامی و جانورشناسی
چکیده انگلیسی
Highly concentrated micellar casein concentrate (HC-MCC), a potential ingredient of protein-fortified food, is a gel at cold temperature. It contains ~17 to 21% casein, with most serum proteins and lactose removed by microfiltration and diafiltration, and it is then further concentrated using vacuum evaporation. The HC-MCC can be stored frozen, and our objective was to determine the conditions needed to obtain complete solubility of thawed HC-MCC in water and to understand its gelation upon cooling. Dispersibility (ability to pass through a 250-µm mesh sieve), suspendability (percentage of protein not sedimented at 80 à g within 5 min), and solubility (percentage of protein not sedimented at 20,000 à g within 5 min) were measured at 4, 12, or 20°C after various mixing conditions. Gelation upon cooling from 50 to 5°C was monitored based on storage (Gâ²) and loss (Gâ²â²) moduli. The gelled HC-MCC was also examined by transmission electron microscopy. Thawed HC-MCC was added to water to reach a protein concentration of 3% and mixed using high shear (7,500 rpm) for 1 min or low shear (800 rpm) for 30 min at 4, 12, 20, or 50°C and at pH 6.4 to 7.2. The HC-MCC completely dispersed at 50°C, or at â¤20°C followed by overnight storage at 4°C. Suspendability at 50°C was ~90% whereas mixing at â¤20°C followed by overnight storage resulted in only ~57% suspendability. Solubility followed a similar trend with ~83% at 50°C and only ~29% at â¤20°C. Mixing HC-MCC with 60 mM trisodium citrate increased dispersibility to 99% and suspendability and solubility to 81% at 20°C. Cold-gelling temperature, defined as the temperature at which Gâ²Â = Gâ²â² when cooling from 50 to 5°C, was positively correlated with protein level in HC-MCC. Gelation occurred at 38, 28, and 7°C with 23, 20, and 17% of protein, respectively. Gelation was reversible upon heating, although after a second cooling cycle the HC-MCC gel had lower Gâ². In micrographs of gelled HC-MCC, the casein micelles were observed to be within the normal size range but packed very closely together, with only ~20 to 50 nm of space between them. We proposed that cold-gelation of HC-MCC occurs when the kinetic energy of the casein micelles is sufficiently reduced to inhibit their mobility in relation to adjacent casein micelles. Understanding solubilization of rehydrated frozen HC-MCC and its rheological properties can help in designing process systems for using HC-MCC as a potential ingredient in liquid food.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Dairy Science - Volume 98, Issue 9, September 2015, Pages 5917-5930
Journal: Journal of Dairy Science - Volume 98, Issue 9, September 2015, Pages 5917-5930
نویسندگان
Y. Lu, D.J. McMahon, L.E. Metzger, A. Kommineni, A.H. Vollmer,