TY - JOUR
T1 - Effect of high pressure on the accumulation of IMP and on the stability of AMP deaminase in rabbit skeletal muscle
AU - Mori, Sunao
AU - Uchida, Akiko
AU - Yamamoto, Shuhei
AU - Sultana, Asma
AU - Tatsumi, Ryuichi
AU - Mizunoya, Wataru
AU - Suzuki, Atsushi
AU - Ikeuchi, Yoshihide
PY - 2007/6/1
Y1 - 2007/6/1
N2 - This study evaluated the effect of high pressure on rabbit skeletal muscle, specifically on the production of inosinic acid (IMP), one of "umami" components, and on the activity of adenosine triphosphate (AMP) deaminase, which plays a role in the conversion of AMP to IMP. By increasing the pressure (0.1 to 300 MPa), nucleotide analysis showed that IMP content in muscle increased instantly with a concomitant decrease in ATP content. The IMP content of muscle at 300 MPa was approximately 15% higher than with lower pressures (0.1-200 MPa) when stored for 1 week at 4C after pressurization. These results suggested that the metabolism of nucleotides in muscle was not significantly impaired by pressure treatment. At 300 MPa, AMP deaminase maintained approximately 70% of the activity at 0.1 MPa. In contrast, the activity of purified AMP deaminase was completely lost at 200 MPa, and irreversible conformational changes were observed by in situ fluorescence spectroscopy. These results indicated that purified AMP deaminase was irreversibly denatured under pressure as high as 300-400 MPa.
AB - This study evaluated the effect of high pressure on rabbit skeletal muscle, specifically on the production of inosinic acid (IMP), one of "umami" components, and on the activity of adenosine triphosphate (AMP) deaminase, which plays a role in the conversion of AMP to IMP. By increasing the pressure (0.1 to 300 MPa), nucleotide analysis showed that IMP content in muscle increased instantly with a concomitant decrease in ATP content. The IMP content of muscle at 300 MPa was approximately 15% higher than with lower pressures (0.1-200 MPa) when stored for 1 week at 4C after pressurization. These results suggested that the metabolism of nucleotides in muscle was not significantly impaired by pressure treatment. At 300 MPa, AMP deaminase maintained approximately 70% of the activity at 0.1 MPa. In contrast, the activity of purified AMP deaminase was completely lost at 200 MPa, and irreversible conformational changes were observed by in situ fluorescence spectroscopy. These results indicated that purified AMP deaminase was irreversibly denatured under pressure as high as 300-400 MPa.
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U2 - 10.1111/j.1745-4514.2007.00118.x
DO - 10.1111/j.1745-4514.2007.00118.x
M3 - Article
AN - SCOPUS:34249998914
SN - 0145-8884
VL - 31
SP - 328
EP - 342
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
IS - 3
ER -