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Method for judging Mactra chinensis protein denaturation based on low-field nuclear magnetic resonance

A low-field nuclear magnetic resonance and protein denaturation technology, which is used in analysis by nuclear magnetic resonance, material analysis by resonance, and measurement devices. simple effect

Pending Publication Date: 2020-04-21
DALIAN POLYTECHNIC UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The disadvantage of using T2 (transverse relaxation) spectrum in the existing technology is that the water distribution position cannot be accurately determined, and only the lateral distribution information of the sample can be obtained, and comprehensive relaxation data cannot be obtained.

Method used

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  • Method for judging Mactra chinensis protein denaturation based on low-field nuclear magnetic resonance
  • Method for judging Mactra chinensis protein denaturation based on low-field nuclear magnetic resonance
  • Method for judging Mactra chinensis protein denaturation based on low-field nuclear magnetic resonance

Examples

Experimental program
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Effect test

Embodiment 1

[0038] A method for judging the denaturation of Chinese clam protein based on low-field nuclear magnetic resonance, comprising steps:

[0039] S1. Low-field NMR analysis: use low-field NMR to collect relaxation information of Chinese clams boiled at 40°C for 2 minutes, use IR-CPMG pulse sequence method to collect NMR echo signals, and invert to obtain echo attenuation curve data, namely Longitudinal relaxation data and transverse relaxation data obtained by multi-exponential fitting;

[0040]Among them, the test conditions are as follows: SF=22, P1=12, O1=392842.53, TD=3675244, PRG=1, TW=5000, P2=25.04, DL2=0.6, NECH=15000, NT1=15, SW=200, RFD=0.08, DRG=3, NS=2;

[0041] S2. Map the transverse relaxation data obtained in step S1 to obtain a T2 relaxation spectrum, map the longitudinal relaxation data to obtain a T1 relaxation spectrum, and combine the T1 relaxation spectrum, T2 relaxation spectrum and NMR 2D Combine the spectra to obtain a two-dimensional spectrum of T1-T2; ...

Embodiment 2

[0046] A method for judging the denaturation of Chinese clam protein based on low-field nuclear magnetic resonance, comprising steps:

[0047] S1. Low-field NMR analysis: Use low-field NMR to collect the relaxation information of Chinese clams processed at 80°C for 2 minutes, then use the IR-CPMG pulse sequence method to collect NMR echo signals, and invert to obtain the echo decay curve data, namely Longitudinal and transverse relaxation data obtained using a multi-exponential fit;

[0048] Among them, the test conditions are as follows: SF=22, P1=12, O1=392842.53, TD=3675244, PRG=1, TW=5000, P2=25.04, DL2=0.6, NECH=15000, NT1=15, SW=200, RFD=0.08, DRG=3, NS=2;

[0049] S2. Map the transverse relaxation data obtained in step S1 to obtain a T2 relaxation spectrum, map the longitudinal relaxation data to obtain a T1 relaxation spectrum, and combine the T1 relaxation spectrum, T2 relaxation spectrum and NMR 2D Combine the spectra to obtain a two-dimensional spectrum of T1-T2; ...

Embodiment 3

[0054] A method for judging the denaturation of Chinese clam protein based on low-field nuclear magnetic resonance, comprising steps:

[0055] S1. Low-field NMR analysis: use low-field NMR to collect the relaxation information of Chinese clams processed at 100°C for 2 minutes, then use the IR-CPMG pulse sequence method to collect NMR echo signals, and invert to obtain the echo decay curve data, namely Longitudinal and transverse relaxation data obtained using a multi-exponential fit;

[0056] Among them, the test conditions are as follows: SF=22, P1=12, O1=392842.53, TD=3675244, PRG=1, TW=5000, P2=25.04, DL2=0.6, NECH=15000, NT1=15, SW=200, RFD=0.08, DRG=3, NS=2;

[0057] S2. Map the transverse relaxation data obtained in step S1 to obtain a T2 relaxation spectrum, map the longitudinal relaxation data to obtain a T1 relaxation spectrum, and combine the T1 relaxation spectrum, T2 relaxation spectrum and NMR 2D Combine the spectra to obtain a two-dimensional spectrum of T1-T2;...

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Abstract

The invention discloses a method for judging Mactra chinensis protein denaturation based on low-field nuclear magnetic resonance. The method adopts low-field nuclear magnetic resonance analysis, acquires echo attenuation curve data of boiled Mactra chinensis by using an IR-CPMG pulse sequence method, processes nuclear magnetic resonance echo signals by using a multi-dimensional function processingmethod to obtain a T1 relaxation spectrogram and a T2 relaxation spectrogram of the Mactra chinensis, and acquires a T1-T2 two-dimensional spectrogram in combination with a nuclear magnetic 2D spectrogram; whether the Mactra chinensis protein is denatured or not is judged according to the T1-T2 two-dimensional spectrogram, and the denaturation standard is that a proportion of a peak area corresponding to the longest transverse relaxation time component is smaller than 4% and the T1 relaxation spectrogram corresponding to the longest transverse relaxation time component has a peak splitting phenomenon. According to the method, the protein denaturation condition can be quickly judged, a new thought can be provided for quality formation in the food processing process, the product maturity isjudged, the processing process is monitored to adjust the processing time, and therefore the product quality is controlled.

Description

technical field [0001] The invention relates to the field of food detection, in particular to a method for detecting the water distribution of Chinese clams by using a low-field nuclear magnetic resonance spectrum, and judging the degree of thermal denaturation based on the information. Background technique [0002] The most important components in aquatic products are water and protein, among which, protein is the supporting structure of aquatic products, and water is the most important component, and it is distributed in various structures in protein. The change and moisture content, distribution and existence state of protein in aquatic products will affect the structure and texture of protein source food. The denaturation of protein will affect the structure and distribution of water, and the change of this protein can be observed intuitively through the water distribution. [0003] At present, the traditional methods of detecting moisture content are mainly dry constan...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): G01N24/08
CPCG01N24/087
Inventor 谭明乾王偲琦陈衍男崔国馨
Owner DALIAN POLYTECHNIC UNIVERSITY
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