Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8415684 | Innovative Food Science & Emerging Technologies | 2018 | 5 Pages |
Abstract
This study was conducted to determine whether the application of ultrahigh pressure could modify the content of inosine 5â²-monophosphate (IMP) in fresh pork and give direct detection of each relevant enzymatic activity to affirm the enzymatic mechanism. Pressure (0-400Â MPa) and time (10Â min) were applied to two types of samples: adenosine monophosphate deaminase, acid phosphatase, and alkaline phosphatase in normal saline and IMP in pork tenderloin. The results showed that varied degrees of susceptibility depended upon the pressure level. The pressure of 300Â MPa could promote the formation of IMP to 1250%, at which the activity of adenosine monophosphate deaminase, an enzyme catalyzing adenosine monophosphate (AMP) to IMP, was maximized. In contrast, the activities of acid phosphatase and alkaline phosphatase were suppressed at this extreme pressure, resulting in decomposition of IMP. Finally, IMP accumulated to its maximum level at 300Â MPa.
Keywords
EDTA (PubChem CID: 6049)IMPAdenosine (PubChem CID: 60961)Potassium hydroxide (PubChem CID: 14797)Perchloric acid (PubChem CID: 24247)Sodium dihydrogen phosphate (PubChem CID: 23672064)Sodium acetate (PubChem CID: 517045)High-pressureEnzyme activityMethanol (PubChem CID: 887)Sodium hydroxide (PubChem CID: 14798)Meat
Related Topics
Life Sciences
Agricultural and Biological Sciences
Food Science
Authors
Zhang Huijuan, Pan Jian, Liang Juan, Xia Xiaoxiao,