Thermal denaturation and aggregation of threadfin bream actomyosin

J. Yongsawatdigul; J. W. Park

doi:10.1016/S0308-8146(03)00105-5

Thermal denaturation and aggregation of threadfin bream actomyosin

J. Yongsawatdigul, J. W. Park

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

211 Citations (Scopus)

Abstract

Threadfin bream (Nemipterus bleekeri) actomyosin formed insoluble aggregates at >40°C. Conformational changes, as measured by surface hydrophobicity, began at >30°C and continued to increase with heating temperature. Reactive sulfhydryl groups increased as heating progressed and decreased at 50°C, indicating the formation of disulfide linkages of threadfin bream actomyosin at >50°C. Two distinct a-helical transition temperatures of actomyosin were found at 36.1 and 47.9°C, while major endothemic transitions were at 38.4, 51.0, and 80.7°C. Storage modulus (G′) started to increase at 34.5°C, implying the simultaneous occurrence of denaturation and aggregation. Gel network formation began to develop at >41°C.

Original language	English
Pages (from-to)	409-416
Number of pages	8
Journal	Food Chemistry
Volume	83
Issue number	3
DOIs	https://doi.org/10.1016/S0308-8146(03)00105-5
Publication status	Published - 2003 Nov

Bibliographical note

Funding Information:
The authors would like to thank the Thailand Research Fund for financially supporting this research under grant RSA/15/2545. The authors also thank Walter A. Baase, Institute of Molecular Biology, University of Oregon, Eugene, OR, USA for technical assistance on circular dichroism measurements.

Keywords

Actomyosin
Aggregation
Thermal denaturation
Threadfin bream

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/S0308-8146(03)00105-5

Cite this

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title = "Thermal denaturation and aggregation of threadfin bream actomyosin",

abstract = "Threadfin bream (Nemipterus bleekeri) actomyosin formed insoluble aggregates at >40°C. Conformational changes, as measured by surface hydrophobicity, began at >30°C and continued to increase with heating temperature. Reactive sulfhydryl groups increased as heating progressed and decreased at 50°C, indicating the formation of disulfide linkages of threadfin bream actomyosin at >50°C. Two distinct a-helical transition temperatures of actomyosin were found at 36.1 and 47.9°C, while major endothemic transitions were at 38.4, 51.0, and 80.7°C. Storage modulus (G′) started to increase at 34.5°C, implying the simultaneous occurrence of denaturation and aggregation. Gel network formation began to develop at >41°C.",

keywords = "Actomyosin, Aggregation, Thermal denaturation, Threadfin bream",

author = "J. Yongsawatdigul and Park, {J. W.}",

note = "Funding Information: The authors would like to thank the Thailand Research Fund for financially supporting this research under grant RSA/15/2545. The authors also thank Walter A. Baase, Institute of Molecular Biology, University of Oregon, Eugene, OR, USA for technical assistance on circular dichroism measurements.",

year = "2003",

month = nov,

doi = "10.1016/S0308-8146(03)00105-5",

language = "English",

volume = "83",

pages = "409--416",

journal = "Food Chemistry",

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T1 - Thermal denaturation and aggregation of threadfin bream actomyosin

AU - Yongsawatdigul, J.

AU - Park, J. W.

N1 - Funding Information: The authors would like to thank the Thailand Research Fund for financially supporting this research under grant RSA/15/2545. The authors also thank Walter A. Baase, Institute of Molecular Biology, University of Oregon, Eugene, OR, USA for technical assistance on circular dichroism measurements.

PY - 2003/11

Y1 - 2003/11

N2 - Threadfin bream (Nemipterus bleekeri) actomyosin formed insoluble aggregates at >40°C. Conformational changes, as measured by surface hydrophobicity, began at >30°C and continued to increase with heating temperature. Reactive sulfhydryl groups increased as heating progressed and decreased at 50°C, indicating the formation of disulfide linkages of threadfin bream actomyosin at >50°C. Two distinct a-helical transition temperatures of actomyosin were found at 36.1 and 47.9°C, while major endothemic transitions were at 38.4, 51.0, and 80.7°C. Storage modulus (G′) started to increase at 34.5°C, implying the simultaneous occurrence of denaturation and aggregation. Gel network formation began to develop at >41°C.

AB - Threadfin bream (Nemipterus bleekeri) actomyosin formed insoluble aggregates at >40°C. Conformational changes, as measured by surface hydrophobicity, began at >30°C and continued to increase with heating temperature. Reactive sulfhydryl groups increased as heating progressed and decreased at 50°C, indicating the formation of disulfide linkages of threadfin bream actomyosin at >50°C. Two distinct a-helical transition temperatures of actomyosin were found at 36.1 and 47.9°C, while major endothemic transitions were at 38.4, 51.0, and 80.7°C. Storage modulus (G′) started to increase at 34.5°C, implying the simultaneous occurrence of denaturation and aggregation. Gel network formation began to develop at >41°C.

KW - Actomyosin

KW - Aggregation

KW - Thermal denaturation

KW - Threadfin bream

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U2 - 10.1016/S0308-8146(03)00105-5

DO - 10.1016/S0308-8146(03)00105-5

M3 - Article

AN - SCOPUS:0041386023

SN - 0308-8146

VL - 83

SP - 409

EP - 416

JO - Food Chemistry

JF - Food Chemistry

IS - 3

ER -

Thermal denaturation and aggregation of threadfin bream actomyosin

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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