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oai:www.ideals.illinois.edu:2142/83672 2023-07-11 col_2142_5131 col_2142_14781 com_2142_5130 com_2142_687 com_2142_397

118 p. Susan Brewer Zhu, Liugen 2015-09-25T21:09:55Z 2015-09-25T21:09:55Z 10000-01-01 2001 2001 From a series of experiments heating metmyoglobin solutions at pHs from 5.0 to 7.0, the effects of temperature and pH on thermal stability of metmyoglobin were investigated. The percent metmyoglobin denatured at temperatures from 25 to 80&deg;C was determined. pHs lower than 6.5 caused metmyoglobin denaturation at various temperatures from 25 to 80&deg;C, but was particularly apparent when pH < 5.6. Metmyoglobin denaturation did not occur until 60&deg;C at pHs from 5.3 to 7.0. It occurred at 55&deg;C at pH 5. A slow heating rate (0.9&deg;C/min) caused more thermal metmyoglobin denaturation than a fast heating rate (1.3&deg;C/min). The denaturation caused by low pH alone was reversible. Made available in DSpace on 2015-09-25T21:09:55Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3017265.pdf: 5034686 bytes, checksum: 54328aa86f43db196326667b20a146ff (MD5) Previous issue date: 2001 Embargo set by: Seth Robbins for item 84953 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001. http://hdl.handle.net/2142/83672 (MiAaPQ)AAI3017265 eng Agriculture, Food Science and Technology Mechanism of Fresh Meat Color and Discoloration text Food Science and Human Nutrition Food Science and Human Nutrition University of Illinois at Urbana-Champaign Dissertation Ph.D.