Thermal stability and denaturation rate of myoglobin from various species of fish

被引:19
作者
Chen, LC [1 ]
Lin, SN [1 ]
Chen, HH [1 ]
机构
[1] Natl Ilan Univ, Dept Food Sci, Ilan, Taiwan
关键词
denaturation; myoglobin; rate constant; thermal stability;
D O I
10.1111/j.1444-2906.2003.00803.x
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
The present study investigated the thermal stability and denaturation rate of myoglobin (Mb) from migratory, demersal, aquaculture and elasmobranch fish species using thermal analysis and dynamic analysis of Mb denaturation. The concentration of Mb was 1.86-2.80 mg/g muscle in the migratory fish, and the tilapia had the lowest Mb concentration of 0.94 mg/g muscle. By analyzing the phase transition temperature (T-m) and denaturation rate of Mb, dolphinfish and horse mackerel Mb showed lower T-m at 46.4 and 51.8degreesC, respectively. The main endothermic peak was around 71.8degreesC for spotted shark Mb. Although the Mb denaturation behaved as biphasic first-order reaction for all the Mb examined, spotted shark Mb showed the highest thermal stability and was followed by chub mackerel and tilapia Mb. The horse mackerel Mb showed the lowest thermal stability.
引用
收藏
页码:293 / 298
页数:6
相关论文
共 23 条
[1]  
[Anonymous], 1985, FOOD CHEM
[2]  
Chang HM, 1992, FOOD SCI, V19, P324
[3]   Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and fluorescence [J].
Chanthai, S ;
Ogawa, M ;
Tamiya, T ;
Tsuchiya, T .
FISHERIES SCIENCE, 1996, 62 (06) :933-937
[4]   Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence [J].
Chanthai, S ;
Ogawa, M ;
Tamiya, T ;
Tsuchiya, T .
FISHERIES SCIENCE, 1996, 62 (06) :927-932
[5]   Decoloration and gel-forming ability of horse mackerel mince by air-flotation washing [J].
Chen, HH .
JOURNAL OF FOOD SCIENCE, 2002, 67 (08) :2970-2975
[6]   Thermal stability and gel-forming ability of shark muscle as related to ionic strength [J].
Chen, HH .
JOURNAL OF FOOD SCIENCE, 1995, 60 (06) :1237-1240
[7]  
Chen M.T., 1989, MEAT SCI TECHNOLOGY, P171
[8]   RELATIONSHIP BETWEEN THE STABILITY AND AUTOXIDATION OF MYOGLOBIN [J].
CHOW, CJ .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1991, 39 (01) :22-26
[9]   The structure and orientation of class-A amphipathic peptides on a phospholipid bilayer surface [J].
Clayton, AHA ;
Sawyer, WH .
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 1999, 28 (02) :133-141
[10]   STRUCTURAL AND FUNCTIONAL-ASPECTS OF THE HEART VENTRICLE MYOGLOBIN OF BLUEFIN TUNA [J].
COLONNA, G ;
IRACE, G ;
BISMUTO, E ;
SERVILLO, L ;
BALESTRIERI, C .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-PHYSIOLOGY, 1983, 76 (03) :481-485