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Penetration Studies of Blood Globin Gels
Author(s) -
AUTIO K.,
LYYTIKÄINEN H.,
MÄLKKI Y.,
KANKO S.
Publication year - 1985
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1985.tb13757.x
Subject(s) - penetration (warfare) , globin , salt (chemistry) , chemistry , chromatography , salt solution , hemoglobin , biochemistry , organic chemistry , operations research , engineering
Studies were made on the effect of temperature, pH and protein and salt concentration on the penetration force withstood by globin gels. The registered force increased with heating temperature (60 ‐ 95°C) and protein concentration (1.4 ‐ 5.0%). The gelation pH was dependent on both protein and salt concentration; the higher the protein or salt concentration the lower the gelation pH. At 3% protein concentration globin formed a gel around pH 5 ‐ 6. At 0.7% concentration and higher, the presence of salt weakened the gel strength, while the addition of plasma increased the gelation pH of salt‐containing globin gels. A substantially higher penetration force was measured for bovine globin gels than porcine globin gels. Further concentration and spray‐drying decreased the gel strength of globin gels.