Effects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle

被引：49

作者：

Choi, Y. M. ^{[1
]}

Ryu, Y. C. ^{[1
]}

Lee, S. H. ^{[1
]}

Go, G. W. ^{[1
]}

Shin, H. G. ^{[1
]}

Kim, K. H. ^{[1
]}

Rhee, M. S. ^{[1
]}

Kim, B. C. ^{[1
]}

机构：

[1] Korea Univ, Coll Life Sci & Biotechnol, Dept Food Sci, Seoul 136701, South Korea

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2008年 / 41卷 / 02期

关键词：

supercritical carbon dioxide; meat quality; protein denaturation;

D O I：

10.1016/j.lwt.2007.02.020

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The objective of this study was to investigate the effect of supercritical carbon dioxide (SC-CO2) treatment for the sterilization purpose on meat quality and protein denaturation of the porcine longissimus dorsi muscle. The conditions Of SC-CO2 treatment were 7.4 and 15.2 MPa at 3 1.1 degrees C for 10 min. SC-CO2 treatment had no effect on muscle pH, tenderness, and water-holding capacity (WHC). However, the samples treated at 7.4MPa had a higher lightness value (52.97 vs. 46.94, P < 0.001) and a more pronounced extent of sarcoplasmic protein denaturation (73.80 vs. 80.73, P < 0.01) than the control samples. These results suggest that the paler color of samples treated with SC-CO2 was associated with the sarcoplasmic protein denaturation, and the major denaturated proteins were determined to be phosphorylase b (PH), creatine kinase (CK), triosephophate isomerase (TPI), and one unknown protein. On the other hand, other quality traits were generally unaffected by the SC-CO2 treatments at 7.4 or 15.2MPa. (0 2007 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.

引用

页码：317 / 322

页数：6

共 28 条

[1] A REVIEW OF THE RELATIONSHIPS OF PH WITH PHYSICAL ASPECTS OF PORK QUALITY [J].

BENDALL, JR ;

SWATLAND, HJ .

MEAT SCIENCE, 1988, 24 (02) :85-126

[2]

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

[3] Effects of high pressure on meat: A review [J].

Cheftel, JC ;

Culioli, J .

MEAT SCIENCE, 1997, 46 (03) :211-236

[4] Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality [J].

Choi, Y. M. ;

Ryu, Y. C. ;

Kim, B. C. .

MEAT SCIENCE, 2007, 76 (02) :281-288

[5] Effect of myosin heavy chain isoforms on muscle fiber characteristics and meat quality in porcine longissimus muscle [J].

Choi, Y. M. ;

Ryu, Y. C. ;

Kim, B. C. .

JOURNAL OF MUSCLE FOODS, 2006, 17 (04) :413-427

[6]

Clifford AA, 2000, METH BIOTEC, V13, P1

[7] Muscle protein gelation by combined use of high pressure/temperature [J].

Colmenero, FJ .

TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2002, 13 (01) :22-30

[8]

Erkmen O, 2000, J SCI FOOD AGR, V80, P1365, DOI 10.1002/1097-0010(200007)80:9<1365::AID-JSFA652>3.3.CO

[9]

2-G

[10] FACTORS AFFECTING POLYACRYLAMIDE-GEL ELECTROPHORESIS AND ELECTROBLOTTING OF HIGH-MOLECULAR-WEIGHT MYOFIBRILLAR PROTEINS [J].

FRITZ, JD ;

SWARTZ, DR ;

GREASER, ML .

ANALYTICAL BIOCHEMISTRY, 1989, 180 (02) :205-210

← 1 2 3 →