CN109061018A - A kind of pre-treating method preventing high protein content matrix gelation - Google Patents
A kind of pre-treating method preventing high protein content matrix gelation Download PDFInfo
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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- G01N30/02—Column chromatography
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Abstract
The invention discloses a kind of pre-treating methods for preventing high protein content matrix gelation, the method is to extraction step in People's Republic of China's standard GB/T/T 22286-2008, GB/T21313-2007 into improving, after buffer salt solution is added at the extraction, step is constant, but in enzymolysis step, C is added18Powder, zinc sulfate are added dropwise a few drop sodium hydroxide solutions, then are centrifuged, and take supernatant, protein-colloid can be thawed or by a large amount of albumen precipitations.It does not select using buffer salt solution at the extraction either, but it is directly extracted with solution of trichloroacetic acid, row enzymolysis step simultaneously, it can effectively solve the problem that supernatant can either melt colloidal state at colloidal state, the step of taking supernatant and adjusting pH can not be carried out according to standard, so that testing result inaccuracy be caused even to detect the problem of can not carrying out.
Description
Technical field
The invention belongs to detection technique fields, and in particular to prevent in the measuring method of beta-receptor agonist residual quantity high
The pre-treating method of the matrix gelation of protein content.
Background technique
GB/T 22286-2008 (the measurement liquid chromatogram string of a variety of beta-receptor agonist residual quantities in animal derived food
Join mass spectrography), GB/T 21313-2007 (beta-receptor agonist method for detecting residue liquid chromatogram-matter in animal derived food
Spectrum/mass spectrography) and No. 1025 bulletin -18-2008 of the Ministry of Agriculture disclosed in beta-receptor excitement in all existing animal derived foods
Agent residue detection includes in the measuring method of the beta-receptors agonist residual quantity such as Liquid Chromatography-Tandem Mass Spectrometry, for animal sources
The matrix that property food is fatty, collagen, protein component are high is carrying out concussion enzymatic hydrolysis, after centrifugation step, needs to take supernatant
Liquid, in the actual operation process, it can be seen that supernatant can at colloidal state either melt colloidal state, can not according to standard into
The step of row takes supernatant and adjusts pH, or in decontaminating column on the later period, it can be because this state be crossed decontaminating column speed and is slowed down, very
To not dripping, cause the even detection of testing result inaccuracy that can not carry out.
Summary of the invention
The present invention provides a kind of pre-treating method of matrix gelation for preventing high protein content, to solve the prior art
Present in the actual operation process supernatant can at colloidal state either melt colloidal state, can not be carried out according to standard
The step of taking supernatant and adjusting pH, or in decontaminating column on the later period, it can be because this state be crossed decontaminating column speed and is slowed down, even
It does not drip, testing result inaccuracy is caused even to detect the problem of can not carrying out.
In order to solve the above technical problems, the present invention adopts the following technical scheme that:
A kind of pre-treating method preventing high protein content matrix gelation, the method are applied in the People's Republic of China (PRC)
In standard GB/T/T 22286-2008, specifically the extraction step in standard is improved, buffering is added at the extraction
After salting liquid, step is constant, but is digesting a step, and C is added18Powder, zinc sulfate are added dropwise a few drop sodium hydroxide solutions, then are centrifuged, and take
Supernatant can thaw protein-colloid or by a large amount of albumen precipitations.Its method particularly includes:
(1) sample of the 2g through smashing to pieces is weighed in 50ml centrifuge tube, and 8ml sodium acetate buffer is added, mixes well, then plus
3.5 drops are added dropwise in 50 μ L β-grape alditol glucoside enzyme/aryl sulfatase and 1g C18 powder, 120g/L solution of zinc sulfate 2mL
1mol/L sodium hydroxide solution, after mixing, 37 DEG C of water-bath oscillation hydrolysis 12h；
(2) the internal standard working solution of 100 μ L 10ng/ml is added in sample to be tested, and capping is placed in horizontal oscillator tube oscillation
15min is centrifuged 10min, takes 4ml supernatant that 0.1mol/L perchloric acid solution 5ml is added, and is uniformly mixed, and adjusts pH with perchloric acid
After being worth 1 ± 0.3,10000r/min refrigerated centrifuge 10min, whole supernatants are transferred in 50ml centrifuge tube, 10mol/L is used
Sodium hydroxide solution adjust pH value to 11,10ml saturated sodium chloride solution is added and 10ml isopropanol-ethyl acetate mixing is molten
Liquid sufficiently extracts, the refrigerated centrifuge 10min at 10000r/min.
The method can also be applied in National Standard of the People's Republic of China GB/T 21313-2007, specific method
Are as follows:
10.0g sample is accurately weighed, acetic acid-acetate buffer that 15ml pH value 5.2 is added is molten, 1000r/min homogenate
1min adds β grape alditol glucoside enzyme/100 μ L and 1g C of aromatic yl acid ester enzyme solutions18Powder, 120g/L solution of zinc sulfate
3-5 drop 1mol/L sodium hydroxide solution is added dropwise in 2mL, digests at 37 DEG C overnight, after taking out cooling, adjusts pH value with perchloric acid
To 1.0, sonic oscillation 20min, taking-up, which is placed in 80 DEG C of water-baths, heats 30min, is put into refrigerator, 10 DEG C of 10000r/min from
Heart 10min pours out supernatant, and it is primary that residue uses 10ml 0.1mol/L perchloric acid solution to extract again, and 10000r/min centrifugation is closed
And supernatant, pH value is adjusted to 4.0 with 1mol/L sodium hydroxide solution, this solution waited for HLB solid-phase extraction column.
And in addition to the above method, the National Standard of the People's Republic of China GB/T 22286-2008 the step of in, mentioning
It does not select using buffer salt solution when taking, but is directly extracted with solution of trichloroacetic acid, while row enzymolysis step, can equally incite somebody to action
Protein-colloid thaws or by a large amount of albumen precipitation.
Step (1) can be with are as follows: weigh sample of the 2g through smashing to pieces in 50m1 centrifuge tube, 15mL10g/L trichlorine be added
Acetic acid solution mixes well, then plus 50 μ L β-grape alditol glucoside enzyme/aryl sulfatase, after mixing, water are vibrated in 37 DEG C of water-baths
Solve 12h.
Similarly, described in commission in magnificent people's republic standard GB/T/T 21313-2007 extraction step
" acetic acid-sodium acetate buffer solution that 15ml pH value 5.2 is added " can also use " 15mL10g/L solution of trichloroacetic acid is added " generation
It replaces, equally can effectively prevent the matrix gelation of high protein content.
The present invention has the advantage that
Inventor has found in the test specifically detected, according to existing GB/T 22286-2008 or GB/T21313-
2007 standards carry out, and the high matrix of, collagen fatty for animal derived food, protein component is carrying out concussion enzyme
It solves, after centrifugation step, needs to take supernatant, in the actual operation process, it can be seen that supernatant can either melt at colloidal state
The step of changing colloidal state, can not carrying out taking supernatant according to these standards and adjust pH, or in decontaminating column on the later period, can be because
Decontaminating column speed is crossed for this state to slow down, or even is not dripped, and testing result inaccuracy is caused even to detect the case where can not carrying out,
In response to this, inventor improves it, and buffer salt solution is added at the extraction, and step is constant, but is digesting
C is added in Cheng Zhong18Powder, zinc sulfate are added dropwise a few drop sodium hydroxide solutions, then are centrifuged, and take supernatant, protein-colloid can be thawed
Or by a large amount of albumen precipitations, thus the problem of effectively preventing aforesaid operations process.
Detailed description of the invention
Fig. 1 is comparison diagram after existing method and the method for the present invention centrifugation.
Specific embodiment
The present invention will be described in detail by specific embodiment below.These embodiments are provided to be to be able to more
Thoroughly understand the present invention, and the scope of the present invention can be fully disclosed to those skilled in the art.
"comprising" or " comprising " as mentioned throughout the specification and claims are an open language, therefore are answered
It is construed to " including but not limited to ".Specification subsequent descriptions are to implement better embodiment of the invention, and so description is
For the purpose of the rule of specification, the range that is not intended to limit the invention.Protection scope of the present invention is when the appended power of view
Benefit requires subject to institute's defender.
Embodiment 1
A kind of pre-treating method preventing high protein content matrix gelation, the method are applied in the People's Republic of China (PRC)
In standard GB/T/T 22286-2008, specifically the extraction step of the sample in standard is improved, at the extraction plus
After entering buffer salt solution, step is constant, but is digesting a step, and C is added18A few drop sodium hydroxide solutions are added dropwise in powder, zinc sulfate, then
Centrifugation, takes supernatant, protein-colloid can be thawed or by a large amount of albumen precipitations.Its method particularly includes:
(1) sample of the 2g through smashing to pieces is weighed in 50ml centrifuge tube, and 8ml sodium acetate buffer is added, mixes well, then plus
3-5 drop is added dropwise in 50 μ L β-grape alditol glucoside enzyme/aryl sulfatase and 1g C18 powder, 120g/L solution of zinc sulfate 2mL
1mol/L sodium hydroxide solution, after mixing, 37 DEG C of water-bath oscillation hydrolysis 12h；
(2) the internal standard working solution of 100 μ L 10ng/ml is added in sample to be tested, and capping is placed in horizontal oscillator tube oscillation
15min is centrifuged 10min, takes 4ml supernatant that 0.1mol/L perchloric acid solution 5ml is added, and is uniformly mixed, and adjusts pH with perchloric acid
After being worth 1 ± 0.3,10000r/min refrigerated centrifuge 10min, whole supernatants are transferred in 50ml centrifuge tube, 10mol/L is used
Sodium hydroxide solution adjust pH value to 11,10ml saturated sodium chloride solution is added and 10ml isopropanol-ethyl acetate mixing is molten
Liquid sufficiently extracts, the refrigerated centrifuge 10min at 10000r/min.
Embodiment 2
A kind of pre-treating method preventing high protein content matrix gelation, the method are applied in the People's Republic of China (PRC)
In standard GB/T/T 22286-2008, its sample extraction method is improved, specifically:
(1) sample of the 2g through smashing to pieces is weighed in 50ml centrifuge tube, and 15mL10g/L solution of trichloroacetic acid is added, it is sufficiently mixed
It is even, then plus 50 μ L β-grape alditol glucoside enzyme/aryl sulfatase, after mixing, 37 DEG C of water-baths oscillation hydrolysis 12h；
(2) the internal standard working solution of 100 μ L 10ng/ml is added in sample to be tested, and capping is placed in horizontal oscillator tube oscillation
15min is centrifuged 10min, takes 4ml supernatant that 0.1mol/L perchloric acid solution 5ml is added, and is uniformly mixed, and adjusts pH with perchloric acid
After being worth 1 ± 0.3,10000r/min refrigerated centrifuge 10min, whole supernatants are transferred in 50ml centrifuge tube, 10mol/L is used
Sodium hydroxide solution adjust pH value to 11,10ml saturated sodium chloride solution is added and 10ml isopropanol-ethyl acetate mixing is molten
Liquid sufficiently extracts, the refrigerated centrifuge 10min at 10000r/min.
Embodiment 3
A kind of pre-treating method preventing high protein content matrix gelation, the method are applied to the People's Republic of China (PRC)
In standard GB/T/T 21313-2007, its extraction step is improved,
Method particularly includes:
10.0g sample is accurately weighed, acetic acid-acetate buffer that 15ml pH value 5.2 is added is molten, 1000r/min homogenate
1min adds β grape alditol glucoside enzyme/100 μ L and 1g C of aromatic yl acid ester enzyme solutions18Powder, 120g/L solution of zinc sulfate
3-5 drop 1mol/L sodium hydroxide solution is added dropwise in 2mL, digests at 37 DEG C overnight, after taking out cooling, adjusts pH value with perchloric acid
To 1.0, sonic oscillation 20min, taking-up, which is placed in 80 DEG C of water-baths, heats 30min, is put into refrigerator, 10 DEG C of 10000r/min from
Heart 10min pours out supernatant, and it is primary that residue uses 10ml 0.1mol/L perchloric acid solution to extract again, and 10000r/min centrifugation is closed
And supernatant, pH value is adjusted to 4.0 with 1mol/L sodium hydroxide solution, this solution waited for HLB solid-phase extraction column.
Embodiment 4
A kind of pre-treating method preventing high protein content matrix gelation, the method are applied to the People's Republic of China (PRC)
In standard GB/T/T 21313-2007, its extraction step is improved, method particularly includes:
10.0g sample is accurately weighed, 15mL10g/L solution of trichloroacetic acid is added, 1000r/min is homogenized 1min, adds
β-grape alditol glucoside enzyme/100 μ L of aromatic yl acid ester enzyme solutions is digested overnight at 37 DEG C, after taking out cooling, is adjusted with perchloric acid
For pH value to 1.0, sonic oscillation 20min, taking-up, which is placed in 80 DEG C of water-baths, heats 30min, is put into refrigerator, 10 DEG C of 10000r/
Min is centrifuged 10min, pours out supernatant, and it is primary that residue uses 10ml 0.1mol/L perchloric acid solution to extract again, 10000r/min from
The heart merges supernatant, adjusts pH value to 4.0 with 1mol/L sodium hydroxide solution, this solution waited for HLB solid-phase extraction column, can be with
The effectively matrix gelation of prevention high protein content.
When dairy products are carried out with the measurement of a variety of beta-receptor agonist residual quantities, marked using GB/T 22286-2008
Method as defined in standard carries out (No. 1), and carries out (No. 2) using the method for the embodiment of the present invention 1, and the two, which compares, sees Fig. 1, in figure
After No. 1 centrifuge tube milk extracting solution centrifugation is taken out, be suspended condensation, filtration difficulty；No. 2 a large amount of albumen precipitations of centrifuge tube in figure
Agglomeration is attached to solution surface layer, is easy to filter and purification run, flow velocity are about 60d/min.
Although above having used general explanation and specific embodiment, the present invention is described in detail, at this
On the basis of invention, it can be made some modifications or improvements, this will be apparent to those skilled in the art.Therefore,
These modifications or improvements without departing from theon the basis of the spirit of the present invention are fallen within the scope of the claimed invention.
Claims (4)
1. a kind of pre-treating method for preventing high protein content matrix gelation, which is characterized in that the method is applied in China
In people's republic's standard GB/T/T 22286-2008, the method specifically:
(1) sample of the 2g through smashing to pieces is weighed in 50ml centrifuge tube, and 8ml sodium acetate buffer is added, mixes well, then plus 50 μ L
β-grape alditol glucoside enzyme/aryl sulfatase and 1g C183.5 drop 1mol/L hydrogen are added dropwise in powder, 120g/L solution of zinc sulfate 2mL
Sodium hydroxide solution, after mixing, 37 DEG C of water-bath oscillation hydrolysis 12h；
(2) the internal standard working solution of 100 μ L 10ng/ml is added in sample to be tested, capping is placed in horizontal oscillator tube oscillation 15min,
Be centrifuged 10min, take 4ml supernatant that 0.1mol/L perchloric acid solution 5ml is added, be uniformly mixed, with perchloric acid adjust pH value to 1 ±
After 0.3,10000r/min refrigerated centrifuge 10min, whole supernatants are transferred in 50ml centrifuge tube, with the hydrogen-oxygen of 10mol/L
Change sodium solution and adjust pH value to 11,10ml saturated sodium chloride solution and 10ml isopropanol-ethyl acetate mixture is added, sufficiently
It extracts, the refrigerated centrifuge 10min at 10000r/min.
2. the pre-treating method of prevention high protein content matrix gelation according to claim 1, which is characterized in that described
Method can also be applied in National Standard of the People's Republic of China GB/T 21313-2007, method particularly includes:
10.0g sample is accurately weighed, acetic acid-acetate buffer that 15ml pH value 5.2 is added is molten, and 1000r/min is homogenized 1min,
Add β -100 μ L and 1g C of grape alditol glucoside enzyme/aromatic yl acid ester enzyme solutions18Powder, 120g/L solution of zinc sulfate 2mL, drop
Add 3-5 drop 1mol/L sodium hydroxide solution, digested at 37 DEG C overnight, take out it is cooling after, adjust pH value to 1.0 with perchloric acid,
Sonic oscillation 20min, taking-up, which is placed in 80 DEG C of water-baths, heats 30min, is put into refrigerator, 10 DEG C of 10000r/min centrifugations
10min pours out supernatant, and it is primary that residue uses 10ml 0.1mol/L perchloric acid solution to extract again, and 10000r/min centrifugation merges
Supernatant adjusts pH value to 4.0 with 1mol/L sodium hydroxide solution, this solution waited for HLB solid-phase extraction column.
3. the pre-treating method of prevention high protein content matrix gelation according to claim 1, which is characterized in that step
It (1) can be with are as follows: sample of the 2g through smashing to pieces is weighed in 50ml centrifuge tube, and 15mL10g/L solution of trichloroacetic acid is added, it is sufficiently mixed
It is even, then plus 50 μ L β-grape alditol glucoside enzyme/aryl sulfatase, after mixing, 37 DEG C of water-baths oscillation hydrolysis 12h.
4. the pre-treating method of prevention high protein content matrix gelation according to claim 2, which is characterized in that China
It is described " acetic acid-second of 15ml pH value 5.2 to be added in people's republic's standard GB/T/T 21313-2007 extraction step
Sour sodium buffer solution " is replaced with " 15mL10g/L solution of trichloroacetic acid is added ".
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111060468A (en) * | 2020-01-19 | 2020-04-24 | 日照健安检测技术服务有限公司 | Method for rapidly detecting protein content in chitin |
| CN112240916A (en) * | 2020-09-03 | 2021-01-19 | 四川佳士特环境检测有限公司 | Method for measuring perchlorate in water |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105699565A (en) * | 2015-06-23 | 2016-06-22 | 山东出入境检验检疫局检验检疫技术中心 | Method and liquid-mass database for detecting residual drugs in animal-derived food |
| CN106404932A (en) * | 2016-08-25 | 2017-02-15 | 罗牛山莱茵检测认证服务（海南）有限公司 | Method for detecting beta-receptor agonist residual quantity in animal derived food |
| CN108490088A (en) * | 2018-03-14 | 2018-09-04 | 汕头出入境检验检疫局检验检疫技术中心 | A kind of detection method of the animal derived product residue of veterinary drug of detection |
-
2018
- 2018-10-19 CN CN201811220061.3A patent/CN109061018A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105699565A (en) * | 2015-06-23 | 2016-06-22 | 山东出入境检验检疫局检验检疫技术中心 | Method and liquid-mass database for detecting residual drugs in animal-derived food |
| CN106404932A (en) * | 2016-08-25 | 2017-02-15 | 罗牛山莱茵检测认证服务（海南）有限公司 | Method for detecting beta-receptor agonist residual quantity in animal derived food |
| CN108490088A (en) * | 2018-03-14 | 2018-09-04 | 汕头出入境检验检疫局检验检疫技术中心 | A kind of detection method of the animal derived product residue of veterinary drug of detection |
Non-Patent Citations (5)
| Title |
|---|
| 中华人民共和国国家质量监督检验检疫总局 中国国家标准化管理委员会: "GB/T 21313-2007 动物源性食品中-受体激动剂残留检测方法 液相色谱-质谱/质谱法", 《中华人民共和国国家标准》 * |
| 中华人民共和国国家质量监督检验检疫总局 中国国家标准化管理委员会: "GB/T 22286-2008 动物源性食品中多种-受体激动剂残留量的测定 液相色谱串联质谱法", 《中华人民共和国国家标准》 * |
| 李丹妮等: "基于液相色谱-串联质谱法同时测定猪和鸡粪便中β-受体激动剂残留的研究", 《饲料研究》 * |
| 梁生旺等: "《中药分析》", 31 December 2016 * |
| 潘煜辰等: "亚临界水萃取及液相色谱－ 串联质谱法检测猪肉中β-受体激动剂与氯霉素残留", 《分析测试学报》 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111060468A (en) * | 2020-01-19 | 2020-04-24 | 日照健安检测技术服务有限公司 | Method for rapidly detecting protein content in chitin |
| CN111060468B (en) * | 2020-01-19 | 2022-08-26 | 日照健安检测技术服务有限公司 | Method for rapidly detecting protein content in chitin sample |
| CN112240916A (en) * | 2020-09-03 | 2021-01-19 | 四川佳士特环境检测有限公司 | Method for measuring perchlorate in water |
| CN112240916B (en) * | 2020-09-03 | 2023-05-30 | 四川佳士特环境检测有限公司 | Method for measuring perchlorate in water |
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Application publication date: 20181221 |