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Characterization of myofibrils cold structural deformation degrees of frozen pork using hyperspectral imaging coupled with spectral angle mapping algorithm.
- Source :
-
Food Chemistry . Jan2018, Vol. 239, p1001-1008. 8p. - Publication Year :
- 2018
-
Abstract
- The study investigated the possibility of using hyperspectral imaging (HSI) in the spectral range of 1000–2200 nm to characterize myofibrils cold structural deformation degrees of frozen pork samples. The HSI images of pork samples frozen under different freezing rates were acquired in the frozen state without thawing. The myofibrils cold structural deformation degrees were evaluated by surface hydrophobicity (S 0 ANS) and Ca 2+ -ATPase activity. Spectral angle mapping (SAM) algorithm was used for the first time to extract the spectral information for regression. Compared with the optimized partial least square regression (PLSR) models based on selected wavebands by successive projections algorithm (SPA), the optimized PLSR models developed based on the spectral angles calculated by the SAM algorithm achieved comparable or even better performance with R 2 P of 0.896 for S 0 ANS and 0.879 for Ca 2+ -ATPase activity, respectively. The implications of the frozen meat spectrum were also analyzed in the current study. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03088146
- Volume :
- 239
- Database :
- Academic Search Index
- Journal :
- Food Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 124878871
- Full Text :
- https://doi.org/10.1016/j.foodchem.2017.07.011