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Chemically stimulated luminescence from food proteins
Author(s) -
CostaLima Bruno,
Zhao Jing,
Boatright William L.
Publication year - 2018
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1002/cche.10106
Subject(s) - luminescence , chemistry , radical , metastability , photochemistry , biochemistry , organic chemistry , materials science , optoelectronics
Background and objectives Protein powders contain metastable radicals that are released upon hydration. The influence of protein source, free radical content, and hydration condition on luminescence was investigated. Findings Hydration of rice, soy, pea, and egg albumin generated a burst of luminescence in the absence of added enhancers/stimulates. Rice proteins were generated from 3 to 10 times more luminescence than other protein samples. Hydrating proteins with 25 mM H 2 O 2 increased the luminescence intensities from all food proteins. Luminescence maximums occurred between 550–600 nm for rice protein, 500–600 nm for soy protein, and two peaks from egg albumin (500–550 nm and <450 nm). Carbon‐centered metastable radicals were most abundant in rice protein which contained between 3.87 × 10 16 –53.44 × 10 16 spins per gram. Plotting intrinsic luminescence versus spins per gram (including all types of proteins examined) revealed an r ‐square of 0.771. Conclusions Based on peak shape, g ‐value (2.0050 ± 0.0003) and power saturation (4–8 mW), metastable radicals in proteins were identified as carbon‐centered. Both intrinsic and added sources of oxidative stimuli strongly correlate with the generation of chemically stimulated luminescence from hydrated proteins. Significance and novelty These findings are the first to correlate the quantity of metastable radicals in rice proteins with intrinsic luminescence generated upon hydration and provide spectral characterization of luminescence from these proteins.