GELATION PROPERTIES OF CHICKEN MYOFIBRILS TREATED WITH CALCIUM AND MAGNESIUM CHLORIDES

Y. L. XIONG; C. J. BREKKE

doi:10.1111/j.1745-4573.1991.tb00438.x

GELATION PROPERTIES OF CHICKEN MYOFIBRILS TREATED WITH CALCIUM AND MAGNESIUM CHLORIDES

Y. L. XIONG, C. J. BREKKE

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

Abstract

Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl₂) and magnesium chloride (MgCl₂). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased (P< 0.05) by CaCl₂ and MgCl₂ and remained constant at 2.5 to 100 mM CaCl₂ and MgCl₂. The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased (P< 0.05) by CaCl₂ but increased (P< 0.05) by MgCl₂. Breast muscle SSP extractability and myofibril gel strength were increased by CaCl₂ and MgCl₂ at less than 5 mM, but were decreased at greater than 10 mM. Tm's of breast muscle SSP were increased (P< 0.05) by MgCl₂ but unchanged (P> 0.05) by CaCl₂. Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl₂ or MgCl₂ but increased at greater concentrations of CaCl₂ or MgCl₂. The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.

Original language	English
Pages (from-to)	21-36
Number of pages	16
Journal	Journal of Muscle Foods
Volume	2
Issue number	1
DOIs	https://doi.org/10.1111/j.1745-4573.1991.tb00438.x
State	Published - Jan 1991

ASJC Scopus subject areas

Food Science

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10.1111/j.1745-4573.1991.tb00438.x

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title = "GELATION PROPERTIES OF CHICKEN MYOFIBRILS TREATED WITH CALCIUM AND MAGNESIUM CHLORIDES",

abstract = "Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl2) and magnesium chloride (MgCl2). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased (P< 0.05) by CaCl2 and MgCl2 and remained constant at 2.5 to 100 mM CaCl2 and MgCl2. The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased (P< 0.05) by CaCl2 but increased (P< 0.05) by MgCl2. Breast muscle SSP extractability and myofibril gel strength were increased by CaCl2 and MgCl2 at less than 5 mM, but were decreased at greater than 10 mM. Tm's of breast muscle SSP were increased (P< 0.05) by MgCl2 but unchanged (P> 0.05) by CaCl2. Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl2 or MgCl2 but increased at greater concentrations of CaCl2 or MgCl2. The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.",

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N2 - Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl2) and magnesium chloride (MgCl2). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased (P< 0.05) by CaCl2 and MgCl2 and remained constant at 2.5 to 100 mM CaCl2 and MgCl2. The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased (P< 0.05) by CaCl2 but increased (P< 0.05) by MgCl2. Breast muscle SSP extractability and myofibril gel strength were increased by CaCl2 and MgCl2 at less than 5 mM, but were decreased at greater than 10 mM. Tm's of breast muscle SSP were increased (P< 0.05) by MgCl2 but unchanged (P> 0.05) by CaCl2. Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl2 or MgCl2 but increased at greater concentrations of CaCl2 or MgCl2. The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.

AB - Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl2) and magnesium chloride (MgCl2). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased (P< 0.05) by CaCl2 and MgCl2 and remained constant at 2.5 to 100 mM CaCl2 and MgCl2. The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased (P< 0.05) by CaCl2 but increased (P< 0.05) by MgCl2. Breast muscle SSP extractability and myofibril gel strength were increased by CaCl2 and MgCl2 at less than 5 mM, but were decreased at greater than 10 mM. Tm's of breast muscle SSP were increased (P< 0.05) by MgCl2 but unchanged (P> 0.05) by CaCl2. Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl2 or MgCl2 but increased at greater concentrations of CaCl2 or MgCl2. The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.

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GELATION PROPERTIES OF CHICKEN MYOFIBRILS TREATED WITH CALCIUM AND MAGNESIUM CHLORIDES

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