CN105779547B - A kind of anti-oxidation peptide mixture and preparation method thereof - Google Patents
A kind of anti-oxidation peptide mixture and preparation method thereof Download PDFInfo
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Abstract
The invention discloses a kind of preparation methods of anti-oxidation peptide mixture, utilize shrimp by-product, it is digested by alpha -chymotrypsin and two step of thermolysin, 1 is obtained through Sephadex G-15 gel chromatography and DEAE Sephacel ion exchange mechansim, 1- diphenyl -2- picryl hydrazine (DPPH) free radical scavenging ability is 10.54 ± 0.03 μm of ol AAE/g pro, and iron ion reducing power (FRAP method) is the anti-oxidation peptide mixture of 89.29 ± 0.01 μm of ol AAE/g pro.The invention also discloses by anti-oxidation peptide mixture obtained by the above method, bulk of molecule 500-1000Da.The present invention provides a kind of new utilization ways for shrimp by-product, reduces resource waste and pollution, improves the commercial value and utilization rate of shrimp by-product.
Description
Technical field
The present invention relates to field of biotechnology, and in particular to a kind of anti-oxidation peptide mixture and its system from shrimp by-product
Preparation Method.
Background technique
Oxidation reaction can generate many detrimental effects to food and biosystem, be to cause food spoilage, nutritional quality
With the major reason of safety decline.In recent years, the purposes of antioxidant was more and more extensive, was applied not only to the oxygen of fat-containing food
Change prevention, and the exploitation as function factor for health food and cosmetics etc..Artificial synthesized antioxidant is because having
Potential side effect and be restricted, therefore food-borne oxidation resistant product more attractive that is natural, having no toxic side effect.It is natural anti-
Oxidation peptide is using food proteins as raw material, by extraction, enzymatic hydrolysis or fermentation, then by isolating and purifying one kind of preparation with anti-
The peptide of oxidation effectiveness.
Protein content accounts for about the 50-60% of dry weight in shrimp by-product, and amino acid classes are complete, has very high nutrition
Value, but it is very low currently with rate.If suitable enzyme can be selected, which to carry out enzymatic hydrolysis to it, prepares anti-oxidation peptide, it will improve shrimp pair
The utility value of product.
Therefore, those skilled in the art is dedicated to by way of digesting and purifying, and utilizes the utilization rates such as shrimp by-product
Protein source low, commercial value is small, prepares anti-oxidation peptide.
Summary of the invention
The present invention provides a kind of anti-oxidation peptide mixture and preparation method thereof from shrimp by-product.Especially by following
Technical solution is realized:
One aspect of the present invention provides a kind of preparation method of anti-oxidation peptide mixture, comprising the following steps:
Shrimp is stripped remaining shrimp head after peeled shrimp and cleans, drying, crushes with shrimp shell by step 1, and sieving obtains shrimp by-product
Powder；
Above-mentioned shrimp by-product powder is added into phosphate buffer for step 2, and dissolution obtains shrimp by-product total protein extraction
Liquid；
Alpha -chymotrypsin is added in step 3, Xiang Shangshu shrimp by-product total protein extracting solution, mixes, is hydrolyzed anti-
It answers；High temperature terminates hydrolysis, and centrifuging and taking supernatant obtains alpha -chymotrypsin enzymolysis liquid；
Thermolysin is added in step 4, Xiang Shangshu alpha -chymotrypsin enzymolysis liquid, mixes, reaction is hydrolyzed；
High temperature terminates hydrolysis, obtains thermolysin enzymolysis liquid；
Step 5, the above-mentioned thermolysin enzymolysis liquid of dialysis, take the component of 500-1000Da in dialyzate；
Step 6 separates the group lease making gel chromatography of above-mentioned 500-1000Da, takes anti-oxidant in gel chromatography separation product
The highest component G of activity1；
Step 7, by said components G1It is separated through anion-exchange chromatography, takes the highest component H of antioxidant activity2。
Further, above-mentioned steps 2 specifically: 0.4g shrimp by-product powder is weighed, is added in 6mL phosphate buffer,
37 DEG C of shaking tables are incubated for 2h, obtain shrimp by-product total protein extracting solution.
Further, above-mentioned steps 3 specifically: 24mg 10000U/ is added into 60mL shrimp by-product total protein extracting solution
Mg alpha -chymotrypsin, whirlpool mix, the hydrolysis 4h at 37 DEG C, terminate hydrolysis at 90 DEG C, are centrifuged, take supernatant,
Obtain alpha -chymotrypsin enzymolysis liquid.
Further, above-mentioned steps 4 specifically: take alpha -chymotrypsin enzymolysis liquid 9.8mL, add 12mg 175U/mL
Thermolysin, whirlpool mix, the hydrolysis 6h at 70 DEG C, terminate hydrolysis at 90 DEG C, obtain thermolysin
Enzymolysis liquid.
Further, in above-mentioned steps 5, dialysis the specific steps are；Thermolysin enzymolysis liquid is put into 1000Da
Cellulose ester membrane bag filter, is immersed in deionized water and dialyses, and the diffusion of components less than 1000Da will contain into deionized water
It is packed into 500Da cellulose ester membrane bag filter, is immersed in after the deionized water rotary evaporation concentration of component less than 1000Da
It dialyses in ionized water, obtains the component of the 500-1000Da in bag and the component less than 500Da outside bag, take 500-1000Da's
Component.
Further, the time dialysed twice is 12h.
Further, above-mentioned steps 6 specifically: by the component of 500-1000Da after rotary evaporation is concentrated, use
The separation of Sephadex G-15 (1.6cm × 90cm) gel filtration chromatography, applied sample amount 1mL；Eluent is deionized water, and flow velocity is
0.5mL/min is collected by every pipe 3mL, is collected 100 pipes altogether, is detected in 214nm；Obtain three component G1-G3, take activity highest
First component G1。
Further, above-mentioned steps 7 specifically: by elution fraction G1Be concentrated after collection, for DEAE Sephacel yin from
Sub- exchange chromatography, applied sample amount 2mL；Eluent is that NaCl solution (is dissolved in 0.05mol/L, pH 8.0Tris-HCl buffer
In), flow velocity 0.8mL/min, every pipe collects 4mL, is eluted by table 1, detect its light absorption value in 214nm；Obtain four groups
Divide H1-H4, second component H2Antioxidant activity it is most strong.
Table 1DEAE Sephacel anion-exchange chromatography elution program
Further, above-mentioned shrimp is Penaeus Vannmei.
Another aspect of the present invention provides the anti-oxidation peptide mixture obtained by above-mentioned preparation method.
Further, the DPPH free radical scavenging ability of above-mentioned anti-oxidation peptide mixture is 10.54 ± 0.03 μm of ol AAE/
G pro, iron ion reducing power are 89.29 ± 0.01 μm of ol AAE/g pro, and bulk of molecule is in anti-oxidation peptide mixture
500-1000Da。
The invention has the following beneficial effects:
(1) protein content is 59.94% ± 0.98% in shrimp by-product powder, is conducive to prepare enzymolysis liquid；
(2) the anti-oxidant enzymolysis liquid that shrimp by-product obtains is digested by alpha -chymotrypsin and two step of thermolysin
DPPH free radical scavenging ability be 10.54 ± 0.03 μm of ol AAE/g pro, iron ion reducing power be 89.29 ± 0.01 μ
Mol AAE/g pro, has stronger anti-oxidation function；
(3) 4h is digested with alpha -chymotrypsin, the degree of hydrolysis of shrimp by-product albumen reaches peak 16.43%；
(4) above-mentioned enzymolysis liquid 6h is digested with thermolysin, the degree of hydrolysis of gained enzymolysis liquid reaches peak, than α-pancreas
Chymotrypsin digests liquid and improves 5.5%；
(5) preparation method provided by the invention is that enzymatic hydrolysis shrimp by-product obtains anti-oxidation peptide mixture, is mentioned for shrimp by-product
A kind of new utilization ways have been supplied, resource waste and pollution is reduced, have improved the commercial value and utilization rate of shrimp by-product；
(6) anti-oxidation peptide mixture provided by the invention derives from food, can be applied in health care product or food；
(7) preparation method step of the invention is simple, can be used for industrial production.
Below with reference to attached drawing, the invention will be further described, with absolutely prove the purpose of the present invention, technical characteristic and
Technical effect.
Detailed description of the invention
Fig. 1 shows in preferred embodiment of the present invention, the antioxidant activity of each component through dialysing；
Fig. 2 a shows in preferred embodiment of the present invention, using Sephadex G-15 gel chromatography chromatography to each component into
214nm absorption value when row is collected；Fig. 2 b shows elution fraction G1-G3Antioxidant activity；
Fig. 3 a is shown in preferred embodiment of the present invention, using DEAE Sephacel anion-exchange chromatography to each component
214nm absorption value and NaCl concentration when being collected；Fig. 3 b shows elution fraction H1-H4Antioxidant activity.
Specific embodiment
With reference to the accompanying drawing and specific embodiment, and the present invention is described in further detail referring to data.It should be understood that these
Embodiment is of the invention solely for the purpose of illustration, rather than limits the range of invention in any way.
Embodiment 1
The pretreatment of step 1 shrimp by-product
Penaeus Vannmei is stripped and is cleaned remaining shrimp head with shrimp shell after peeled shrimp, is placed in thermostatic drying chamber and dries for 60 DEG C
16h is crushed with Multifunctional pulverizers, and crosses 60 meshes.
The determination of step 2 shrimp by-product total protein optimum extraction time
The shrimp shell meal of 0.4g is weighed, is added in 6mL phosphate buffer (0.05mol/L, pH 8.0), 37 DEG C of shaking table difference
It is incubated for 0.25,0.5,0.75,1,1.5,2,3,4 and 6h.Utilize Bradford kit measurement total protein liquid concentration.As a result table
Bright, with the growth of extraction time in 0-2h, water-soluble shrimp protein concentration is gradually increasing, and water solubility shrimp protein concentration reaches when 1.5h
Water solubility shrimp protein concentration is 23.49% when to 23.14%, 2h.Hereafter the water-soluble shrimp protein concentration that 3,4 and 6h is obtained is without aobvious
It writes and increases, therefore choosing 2h is shrimp protein extraction time.
The measurement of step 3 degree of hydrolysis
The measurement of degree of hydrolysis (DH) is with reference to Adler-Nissen method and modifies: taking 0.1mL enzymolysis liquid sample in examination
Guan Zhong, is added 2.2mL phosphate buffer (0.05mol/L, pH 8.2) and 2mL 0.1%TNBS solution mixes, and 50 DEG C are protected from light
Water-bath 1h.4mL 0.1mol/L hydrochloric acid is added and terminates reaction, is stored at room temperature 30min, measures mixed liquor light absorption value in 340nm.With
The L-Leu of various concentration substitutes sample, makees standard curve.It calculates according to the following formula:
In formula: htFor amino nitrogen concentration (mmol/g) after reaction；h0To react preceding amino nitrogen concentration (mmol/g)；htot
For the peptide bond mM number (mmol/g) of every gram of material protein, the h of shrimp by-producttot=8.073mmol/g.
The optimization of step 4 alpha -chymotrypsin enzymatic hydrolysis condition
24mg alpha -chymotrypsin (10000U/mg) is added into protein extract described in step 2, is vortexed and mixes,
0,1,2,3,4,5 and 6h is successively hydrolyzed under 37 DEG C of constant temperature.Then 90 DEG C of water-bath 15min terminate reaction, and in 5000rpm revolving speed
Lower centrifugation 5min, takes supernatant, obtains the alpha -chymotrypsin enzymolysis liquid hydrolyzed by different time (every group three parallel).It adopts
The method described in step 3 measures degree of hydrolysis, the results showed that, with the growth of time in 0-4h, DH is gradually increased, the DH in 4h
It is 16.49% when reaching 16.43%, 6h, the two is without significant difference.Therefore when selecting 4h as alpha -chymotrypsin optimum hydrolysis
Between, prawn by-product carries out batch hydrolysis, and alpha -chymotrypsin enzymolysis liquid is placed in -20 DEG C of preservations.
The optimization of step 5 thermolysin enzymatic hydrolysis condition
The above-mentioned alpha -chymotrypsin enzymolysis liquid 9.8mL digested by 4h is taken, 12mg thermolysin, mixing are added
Uniformly, after 70 DEG C digest 1,2,4,6 and 8h respectively, 90 DEG C of water-bath 15min terminate reaction, obtain thermolysin enzymatic hydrolysis
Liquid.Degree of hydrolysis is measured using method described in step 3, the results showed that, in 0-6h, with the growth of time, DH is gradually increasing, 6h
Variation is little afterwards.It is 5.6% when DH reaches 5.5%, 8h when 6h, therefore selecting 6h is best enzymolysis time, batch prepares Thermophilic Bacteria
Protease hydrolyzed liquid.
Step 6 anti-oxidation peptide isolates and purifies
(1) above-mentioned thermolysin enzymolysis liquid is concentrated 5 times by rotary evaporation by dialysis, and concentrate is put into 1000Da
Cellulose ester membrane bag filter, then it is immersed in the beaker for filling deionized water, and be stirred using magnetic stirring apparatus.When dialysing total
A deionized water is changed when a length of 12h, every 6h.After dialysis, the component greater than 1000Da is stayed in bag filter.Less than 1000Da's
Diffusion of components is concentrated into deionized water, and through rotary evaporation, is packed into 500Da cellulose ester membrane bag filter, repeats above-mentioned
Dialysis procedure.It is dialysed by this, the component of 500-1000Da stays in bag filter；Diffusion of components less than 500Da to go from
Sub- water, after concentrated by rotary evaporation, measurement activity respectively.As a result as shown in Figure 1, the component of 500-1000Da has highest anti-oxidant work
Property.
(2) gel permeation chromatography Sephadex G-15 filler is suitable for 1500Da small molecule progress chromatography below.
By the gel-filled chromatographic column into 1.6 × 90cm, with deionized water to chromatography column equilibration 12h after, add 1mL to dialyse resulting 500-
1000Da sample.Eluent is deionized water, and flow velocity 0.5mL/min is collected by every pipe 3mL, 100 pipes is collected altogether, in 214nm
Detection.As shown in Figure 2 a, 3 component G are obtained1-G3.Each component is collected, activity is measured after rotary evaporation concentration, as a result as schemed
Shown in 2b, component G1Antioxidant activity highest.
(3) filler DEAE Sephacel is filled into 2.5 × 8cm glass chromatography column by ion-exchange chromatography, uses 0.05mol/
L, pH 8.0Tris-HCl buffer are balanced column, until efflux is consistent with the pH value of influent.Take 2mL G1Component
It is loaded, flow velocity 0.8mL/min, every pipe collects 4mL, eluted by table 1, detect its light absorption value in 214nm.As a result such as
Shown in Fig. 3 a, 4 component H are obtained1-H4.Each component is collected, rotary evaporation concentration detection is active, as a result as shown in Figure 3b, group
Divide H2Antioxidant activity highest, DPPH free radical scavenging ability (AAE) based on ascorbic acid is 10.54 ± 0.03 μm of ol
AAE/g pro, iron ion reducing power are 89.29 ± 0.01 μm of ol AAE/g pro.
Embodiment 2
The Antioxidative Activity Determination of anti-oxidation peptide mixture obtained in embodiment 1
The measurement of step 1DPPH free radical scavenging activity: replace sample as the positive using ascorbic acid and deionized water respectively
And negative control group.DPPH solution is prepared: 3mg DPPH is added in 100mL methanol, is sufficiently dissolved.1mL sample is taken, is added
30min is placed in the DPPH solution of 4mL, room temperature darkroom, and light absorption value is measured at 517nm.The ascorbic acid of various concentration is set, and
Draw standard curve.DPPH free radical scavenging activity is calculated as follows:
In formula: A1For the absorbance value for adding DPPH solution after hydrolyzate；A2For the absorbance value of hydrolyzate；A3Not add water
The absorbance value of DPPH solution when solving liquid.
The measurement of step 2 iron ion reducing power: replace sample as positive and yin using ascorbic acid and deionized water respectively
Property control group, every group of setting three are parallel.It takes 0.5mL sample in 10mL centrifuge tube, is then separately added into 0.5mL phosphoric acid buffer
Liquid (pH 6.6), the potassium ferricyanide solution of 0.5mL 1% and whirlpool concussion mix.Centrifuge tube is placed in water-bath, 50 DEG C of water
Bathe 20min.After the water bath is over, centrifuge tube taking-up is quickly cooled down under condition of ice bath rapidly.0.5mL tri- is added into centrifuge tube
Chloroacetic acid solution, concussion mix.The liquor ferri trichloridi (being dissolved in 3.5% hydrochloric acid) and 4mL of 0.8mL 0.1% is then added
Deionized water simultaneously mixes, and stands 10min under room temperature.Measure light absorption value of the sample at 700nm.
Implementation result: under this experiment condition, the DPPH free radical scavenging ability of anti-oxidation peptide mixture is 10.54 ±
0.03 μm of ol AAE/g pro, iron ion reducing power are 89.29 ± 0.01 μm of ol AAE/g pro, anti-oxidation peptide mixture point
The size of son is 500-1000Da.
The preferred embodiment of the present invention has been described in detail above.It should be appreciated that the ordinary skill of this field is without wound
The property made labour, which according to the present invention can conceive, makes many modifications and variations.Therefore, all technician in the art
Pass through the available technology of logical analysis, reasoning, or a limited experiment on the basis of existing technology under this invention's idea
Scheme, all should be within the scope of protection determined by the claims.
Claims (8)
1. a kind of preparation method of anti-oxidation peptide mixture, which is characterized in that the preparation method comprises the following steps:
Shrimp is stripped remaining shrimp head after peeled shrimp and cleans, drying, crushes with shrimp shell by step 1, and sieving obtains shrimp by-product powder；
The shrimp by-product powder is added into phosphate buffer for step 2, and dissolution obtains shrimp by-product total protein extracting solution；
24mg 10000U/mg alpha -chymotrypsin, whirlpool are added into shrimp by-product total protein extracting solution described in 60mL for step 3
Whirlpool mixes, the hydrolysis 4h at 37 DEG C, terminates hydrolysis at 90 DEG C, is centrifuged, takes supernatant, obtain the α-chymotrypsin protein
Enzyme enzymolysis liquid；
Thermolysin is added in step 4, Xiang Suoshu alpha -chymotrypsin enzymolysis liquid, mixes, reaction is hydrolyzed；High temperature
Hydrolysis is terminated, thermolysin enzymolysis liquid is obtained；
Step 5, the dialysis thermolysin enzymolysis liquid, take the component of 500-1000Da in dialyzate；The specific step of dialysis
Suddenly it is；The thermolysin enzymolysis liquid is put into 1000Da cellulose ester membrane bag filter, is immersed in deionized water and dialyses,
Diffusion of components less than 1000Da will contain less than the deionized water rotary evaporation concentration of the component of 1000Da into deionized water
It is packed into 500Da cellulose ester membrane bag filter afterwards, is immersed in deionized water and dialyses, obtain the component of the 500-1000Da in bag
The component less than 500Da with outside bag, takes the component of the 500-1000Da；
Step 6 separates the group lease making gel chromatography of the 500-1000Da, takes antioxidant activity in gel chromatography separation product
Highest component G1；
Step 7, by the component G1Through ion exchange mechansim, the highest component H of antioxidant activity is taken2。
2. preparation method according to claim 1, which is characterized in that the step 2 specifically: weigh 0.4g shrimp by-product
Powder is added in 6mL phosphate buffer, and 37 DEG C of shaking tables are incubated for 2h, obtains the shrimp by-product total protein extracting solution.
3. preparation method according to claim 1, which is characterized in that the step 4 specifically: take the α-pancreas curdled milk egg
White enzyme enzymolysis liquid 9.8mL adds 12mg 175U/mL thermolysin, and whirlpool mixes, the hydrolysis 6h at 70 DEG C, and 90 DEG C
Lower termination hydrolysis obtains the thermolysin enzymolysis liquid.
4. preparation method according to claim 1, which is characterized in that the time dialysed twice is 12h.
5. preparation method according to claim 1, which is characterized in that the step 6 specifically: by the 500-1000Da
Component after rotary evaporation is concentrated, with Sephadex G-15 gel filtration chromatography separate, obtain three component G1-G3, take work
The highest first component G of property1。
6. preparation method according to claim 1, which is characterized in that the shrimp is Penaeus Vannmei.
7. the anti-oxidation peptide mixture that preparation method according to claim 1 to 6 obtains.
8. anti-oxidation peptide mixture according to claim 7, which is characterized in that the DPPH of the anti-oxidation peptide mixture is certainly
It is 10.54 ± 0.03 μm of ol AAE/g pro by base Scavenging activity, iron ion reducing power is 89.29 ± 0.01 μm of ol AAE/g
Pro, bulk of molecule is 500-1000Da in the anti-oxidation peptide mixture.
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102676623A (en) * | 2012-05-23 | 2012-09-19 | 浙江大学 | Method for preparing antioxidant peptide from shrimp shell |
| CN104558105A (en) * | 2015-01-04 | 2015-04-29 | 华南理工大学 | Antioxidative peptide of metapenaeus affinis as well as separation and extraction method and application of antioxidative peptide |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102676623A (en) * | 2012-05-23 | 2012-09-19 | 浙江大学 | Method for preparing antioxidant peptide from shrimp shell |
| CN104558105A (en) * | 2015-01-04 | 2015-04-29 | 华南理工大学 | Antioxidative peptide of metapenaeus affinis as well as separation and extraction method and application of antioxidative peptide |
Non-Patent Citations (2)
| Title |
|---|
| 活性肽构效关系的研究进展;朱蕴菡;《中华中医药杂志(原中国医药学报)》;20121031;第27卷(第10期);第2626页左栏第4段至右栏第3段 |
| 虾头虾壳蛋白质酶解制备抗氧化肽的研究;张风;《南方水产科学》;20151231;第11卷(第6期);摘要 |
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