Ca2+ affects physicochemical and conformational changes of threadfin bream myosin and actin in a setting model

被引：41

作者：

Hemung, BO ^{[1
]}

Yongsawatdigul, J ^{[1
]}

机构：

[1] Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand

来源：

JOURNAL OF FOOD SCIENCE | 2005年 / 70卷 / 08期

关键词：

threadfin bream; myosin; actin; calcium; setting;

D O I：

10.1111/j.1365-2621.2005.tb11500.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The effect of Ca2+ on physicochemical and conformational changes of threadfin bream (TB) myosin and actin during setting at 25 and 40 degrees C was investigated. Ca2+ ion at 10 to 100 mM induced the unfolding of myosin and. actin as evident by an increase of surface hydrophobicity (S(o)ANS) at 40 degrees C. Total SH groups also decreased with an increased Call concentration, suggesting that Ca2+ promoted the formation of disulfide bonds during setting at 40 degrees C.Both hydrophobic interactions and disulfide linkages were involved in formation of myosin aggregates at 40 degrees C and were enhanced by addition of 10 to 100 mM Ca2+. Myosin Ca-ATPase activity decreased when Ca2+ was greater than 50 mM, indicating conformational changes of myosin head. Circular dichroism spectra demonstrated that Ca2+ reduced the a-helical content of myosin and actin incubated at either 25 or 40 degrees C. Ca2+ induced conformational changes of TB myosin and actin incubated at 40 degrees C to a greater extent than at 25 degrees C.

引用

页码：C455 / C460

页数：6

共 30 条

[1] MECHANISM OF PROTEIN SALTING IN AND SALTING OUT BY DIVALENT-CATION SALTS - BALANCE BETWEEN HYDRATION AND SALT BINDING [J].

ARAKAWA, T ;

TIMASHEFF, SN .

BIOCHEMISTRY, 1984, 23 (25) :5912-5923

[2] How Hofmeister ion interactions affect protein stability [J].

Baldwin, RL .

BIOPHYSICAL JOURNAL, 1996, 71 (04) :2056-2063

[3] CORRELATION AMONG THE PROTON CHARGES AND MOLECULAR MASSES OF MYOSIN SUBUNITS [J].

BECHET, JJ ;

DALBIS, A .

FEBS LETTERS, 1989, 249 (01) :8-12

[4] Suwari gel properties as affected by transglutaminase activator and inhibitors [J].

Benjakul, S ;

Visessanguan, W ;

Pecharat, S .

FOOD CHEMISTRY, 2004, 85 (01) :91-99

[5]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[6] Herring surimi during low temperature setting, physicochemical and textural properties [J].

Chan, JK ;

Gill, TA ;

Thompson, JW ;

Singer, DS .

JOURNAL OF FOOD SCIENCE, 1995, 60 (06) :1248-1253

[7] TISSUE SULFHYDRYL GROUPS [J].

ELLMAN, GL .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) :70-77

[8] EFFECT OF SALT CONCENTRATION AND TEMPERATURE ON HEAT-INDUCED AGGREGATION AND GELATION OF FISH MYOSIN [J].

GILL, TA ;

CHAN, JK ;

PHONCHAREON, KF ;

PAULSON, AT .

FOOD RESEARCH INTERNATIONAL, 1992, 25 (05) :333-341

[9] CALCIUM-BINDING AND SALT-INDUCED STRUCTURAL-CHANGES OF NATIVE AND PREHEATED BETA-LACTOGLOBULIN [J].

JEYARAJAH, S ;

ALLEN, JC .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1994, 42 (01) :80-85

[10] NONDISULFIDE COVALENT CROSS-LINKING OF MYOSIN HEAVY-CHAIN IN SETTING OF ALASKA POLLOCK AND ATLANTIC CROAKER SURIMI [J].

KAMATH, GG ;

LANIER, TC ;

FOEGEDING, EA ;

HAMANN, DD .

JOURNAL OF FOOD BIOCHEMISTRY, 1992, 16 (03) :151-172

← 1 2 3 →