Title of article :
Exploration of the Use of NIR Reflectance Spectroscopy to Distinguish and Measure Attributes of Conditioned and Cooked Shrimp (Pandalus borealis)
Author/Authors :
Brodersen، K. نويسنده , , Bremner، H. A. نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2001
Abstract :
The oxidative polymerisation of tyrosinyl residues in wheat gliadin by mushroom tyrosinase was studied. After gliadin had been incubated with mushroom tyrosinase, conjugation and SS linking were observed by SDS-PAGE. The reaction mixture of gliadin treated with mushroom tyrosinase was then analysed by size-exclusion high-performance liquid chromatography (SE-HPLC). While the peak area of fraction 5 (MW 20-60 kDa) had decreased after gliadin had been incubated with mushroom tyrosinase for 3 h, the relative peak area of fraction 2 (MW 350 kDa-1,000kDa) had increased from 8.5% to 27.0% compared with the control. There was no change in the relative area of fractions 3 (MW 130-350 kDa), 4 (MW 60 kD-130 kDa) and 6 (MW<20 kDa) during incubation with mushroom tyrosinase. Protein-bound 5- S -cysteinyl-3, 4-dihydroxyphenylalanine (5- S cysteinyldopa) in the gliadin incubated with mushroom tyrosinase was observed to increase with increasing incubation time and amount of mushroom tyrosinase. More protein-bound 5- S cysteinyldopa was formed in the 70% ethanol-insoluble fraction than in the 70% ethanol-soluble fraction at 5°C. It is suggested that the formation of protein-bound 5- S -cysteinyldopa from the tyrosinyl and cysteinyl residues of wheat gliadin can lead to intra- and intermolecular bonding of protein.
Keywords :
near infrared reflectance , NIR , shrimp , Pandalus borealis
Journal title :
LEBENSMITTELWISSENSCHAFT & TECHNOLOGYE / FOOD SCIENCE
Journal title :
LEBENSMITTELWISSENSCHAFT & TECHNOLOGYE / FOOD SCIENCE