Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Y. L. XIONG; E. A. DECKER; G. H. ROBE; W. G. MOODY

doi:10.1111/j.1365-2621.1993.tb06156.x

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Y. L. XIONG, E. A. DECKER, G. H. ROBE, W. G. MOODY

Animal and Food Sciences

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

75 Scopus citations

Abstract

Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range 5.8–7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.

Original language	English
Pages (from-to)	1241-1244
Number of pages	4
Journal	Journal of Food Science
Volume	58
Issue number	6
DOIs	https://doi.org/10.1111/j.1365-2621.1993.tb06156.x
State	Published - Nov 1993

Keywords

antioxidation
beef
gelation
heart
myofibrils

ASJC Scopus subject areas

Food Science

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10.1111/j.1365-2621.1993.tb06156.x

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title = "Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions",

abstract = "Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range 5.8–7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.",

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year = "1993",

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T1 - Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

AU - XIONG, Y. L.

AU - DECKER, E. A.

AU - ROBE, G. H.

AU - MOODY, W. G.

PY - 1993/11

Y1 - 1993/11

N2 - Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range 5.8–7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.

AB - Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range 5.8–7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.

KW - antioxidation

KW - beef

KW - gelation

KW - heart

KW - myofibrils

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Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

Abstract

Keywords

ASJC Scopus subject areas

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