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High-pressure effects on the mechanism of accumulated inosine 5′-monophosphate
Innovative Food Science & Emerging Technologies ( IF 6.3 ) Pub Date : 2017-12-16 , DOI: 10.1016/j.ifset.2017.12.005
Zhang Huijuan , Pan Jian , Liang Juan , Xia Xiaoxiao

This study was conducted to determine whether the application of ultrahigh pressure could modify the content of inosine 5′-monophosphate (IMP) in fresh pork and give direct detection of each relevant enzymatic activity to affirm the enzymatic mechanism. Pressure (0–400 MPa) and time (10 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 300 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 300 MPa.



中文翻译:

高压对肌苷5'-单磷酸积累机理的影响

本研究旨在确定施加超高压是否可以改变鲜猪肉中肌苷5'-单磷酸(IMP)的含量,并直接检测每种相关的酶促活性以确认酶促机理。对两种类型的样品施加压力(0–400 MPa)和时间(10分钟):生理盐水中的腺苷单磷酸脱氨酶,酸性磷酸酶和碱性磷酸酶以及猪里脊肉中的IMP。结果表明,不同程度的磁化率取决于压力水平。300 MPa的压力可以促使IMP的形成达到1250%,此时,单磷酸腺苷(AMP)催化IMP的酶的活性得以最大化。相比之下,在此极端压力下,酸性磷酸酶和碱性磷酸酶的活性受到抑制,导致IMP分解。最终,IMP累积到300 MPa的最高水平。

更新日期:2017-12-16
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