Effects of high temperature aging upon certain characteristics
of bovine l. dorsi muscle were studied. Paired wholesale ribs of
carcasses were obtained subsequent to slaughter. The left rib of
each pair was held at 30°C for 24 hours, then stored at 3°C.
Analogous right ribs were immediately stored at 3°C. A sampling
schedule of 0, 1, 2, 3, 4, 7, and 10 days was followed.
Muscles held at only the 3°C temperature showed slightly
higher pH levels and superior water binding capacity than those
subjected to the high temperature aging treatment.
Up to three days storage, extractability of water soluble protein
was greatest from muscles held at the elevated temperature. After
the third day, however, extractability was greater for muscles held
at 3°C. Also during the first three days of aging, tyrosine-
tryptophan index ratios indicated protein breakdown to be greatest
in muscles subjected to the elevated temperature. Thereafter, proteolysis appeared to occur more rapidly in the muscles held at
3°C.
Color differences between muscles treated via the two storage
temperatures were marked. Spectrophotometric ratios (422/280 mμ)
of extracts showed that muscles held at the high temperature had
higher extractable levels of oxymyoglobin than ribs held at 3°C.
This difference remained apparent throughout the aging period.
Results of DEAE-cellulose ion exchange chromatography of
the sarcoplasmic proteins showed only minor variations in profiles
between the two aging treatments. Alterations did appear with time.
Profile alterations did not appear related to anticipated increases in
tenderness. / Graduation date: 1967
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/27011 |
| Date | 19 January 1967 |
| Creators | Thompson, Garet Barton |
| Contributors | Anglemier, Allen F. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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