z-logo
Premium
Investigation of contributors to zinc protoporphyrin IX formation at optimum pH 5.5 in pork
Author(s) -
Akter Mofassara,
Shiraishi Akiko,
Kumura Haruto,
Hayakawa Toru,
Wakamatsu Junichi
Publication year - 2019
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.13201
Subject(s) - myoglobin , chemistry , fraction (chemistry) , protoporphyrin , size exclusion chromatography , ultrafiltration (renal) , zinc , chromatography , biochemistry , zinc protoporphyrin , heme , organic chemistry , enzyme , porphyrin
Abstract We investigated zinc protoporphyrin (ZnPP) formation in pork at pH 5.5, identified the contributors to ZnPP formation, and verified the involvement of myoglobin in this process. When pork homogenate was separated into two water‐soluble fractions (>10 and <10 kDa) and an insoluble fraction, ZnPP formation was suppressed. ZnPP formation was rescued after mixing of all three fractions. Heating of the soluble <10 kDa fraction did not suppress the formation of ZnPP as opposed to heating of the soluble >10 kDa fraction, suggesting that protein(s) presents in the >10 kDa fraction contributed to ZnPP formation. Components of the soluble 10–30 kDa fractions separated by ultrafiltration were important in ZnPP formation. Exogenous myoglobin was not essential for ZnPP formation. A gel filtration study showed that soluble protein(s) with molecular weight higher than that of myoglobin was involved. Therefore, it was suggested that the soluble <10 kDa fraction, the insoluble fraction, and the soluble 10–30 kDa fraction (excluding myoglobin) are essential for ZnPP formation in pork at pH 5.5.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here