CN105648006A - Preparation method of dasyatis akajei chondroprotein antioxidative peptide - Google Patents
Preparation method of dasyatis akajei chondroprotein antioxidative peptide Download PDFInfo
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Abstract
The invention discloses a preparation method of a dasyatis akajei chondroprotein antioxidative peptide. The method comprises: taking dasyatis akajei cartilage as a raw material; performing total protein extraction, acetone fractional precipitation, and trypsin enzymolysis to obtain an enzymatic hydrolysate; and separating and purifying the enzymatic hydrolysate through ultrafiltration, ion exchange resin chromatography, gel column chromatography, and reversed-phase high-performance liquid chromatography to obtain the antioxidative peptide Ile-Glu-Pro-His having a molecular weight of 494.55 Da measured through ESI-MS. The prepared high-activity antioxidative peptide has an excellent scavenging effect on DPPH free radicals, hydroxyl free radicals, ABTS free radicals, and superoxide anionic free radicals and has an excellent inhibiting effect on lipid peroxidation. The antioxidative peptide is safe, has no toxic or side effect, and is high in antioxidant activity and easy to absorb and digest. The antioxidant activity can be used as a medicine, a health food, or a food additive.
Description
Technical field
The preparation method that the present invention relates to a kind of animal cartilage albumen, the preparation method being specifically related to a kind of red chondroprotein anti-oxidation peptide.
Background technology
Red (Dasyatisakajei), belongs to Chondrichthyes, lower opening catalogue, Myliobatiformes, section, belongs to. Red for common cartilaginous fish, it is distributed in China coast, also sees the Xijiang River, until Nanning, Longzhou, Guiping, and Japan, the Korea peninsula.
Red for the conventional marine drug of China, book on Chinese herbal medicine is practised and claims Carnis Dasyatis akajei, begin to be loaded in supplement to the Herbal. Red whole body is precious, and its meat, tooth, anal spine etc. all can be used as medicine. Red meat has nourishing YIN and supplementing blood, and kidney tonifying is treating stranguria. Cure mainly dysuria, puckery pain, man's nebulousurine stranguria marked by chyluria, infantile malnutrition. Red tooth has the effects such as parasite killing, preventing the attack (or recurrence) of malaria, removing toxic substances, it is possible to the diseases such as treatment miasma is cruel, pruritus. Red liver has the effects such as nourishing the liver to improve visual acuity, strengthening by means of tonics, bone strengthening. Red anal spine is poisonous, has the effects such as heat-clearing and toxic substances removing, pain relieving, hard masses softening and resolving. Red fish oil is slightly poisonous, has the effects such as strengthening by means of tonics, blood activating and fat reducing. And modern pharmacology also demonstrates that the red multiple significant pharmacologically active that has, red cartilage mucopolysaccharide have good anticoagulant active and effect for reducing blood fat, with existing anticoagulation medicine activity quite; Red anal spine 20% ethanol extraction can suppress the growth of mouse S 180 sarcoma, and the polypeptide that red cartilage extracts can substantially reduce the number of the blood capillary of Murine Hepatoma22 and the number of chick chorioallantoic membrane new vessels.
Summary of the invention
The technical problem to be solved be the present situation for prior art provide a kind of can the preparation method of red chondroprotein anti-oxidation peptide of scavenging free radicals and anti-lipid peroxidation effect.
The present invention solves that the technical scheme that above-mentioned technical problem is taked is: the preparation method of a kind of red chondroprotein anti-oxidation peptide, it comprises the following steps:
1) preparation of red cartilage total protein crude extract: weigh Raja porosa cartilage and be cut into fine grained chippings, add appropriate distilled water, in high-speed tissue mashing machine, homogenate is to pasty state, the red cartilage of pasty state is dipped in the 1.0mol/L guanidine hydrochloride solution of 4��6 times of volumes (containing 0.02mol/LMES and 0.02mol/LEDTA, pH7��8), at 4 DEG C, stir extracting 36��48h.Extracting solution with the centrifugal 15��25min of 4000��6000r/min, is abandoned residue and is collected supernatant at 4 DEG C; Supernatant continues, at 4 DEG C, the centrifugal 15��25min of 10000��12000r/min, to take supernatant and remove insoluble impurities with 0.22 ��m of filtering with microporous membrane. Filtrate being loaded in the bag filter that molecular retention amount is 8000, with Tris-HCl(pH7.6) buffer dialyses 24��48h at 4 DEG C, and in bag filter, solution is red cartilage total protein crude extract.
) preparation of red cartilage acetone fractional precipitation albumen: taking red cartilage total protein crude extract, to be slowly added to pre-cold acetone to acetone concentration under ice bath be 30%, after standing 4��6h at-20 DEG C, in 4 DEG C, 10000��12000r/min high speed centrifugation 20min, take supernatant, adding pre-cold acetone to the final acetone concentration of solution is 60%, obtain red cartilage 60% acetone precipitation albumen, lyophilizing, be 60% acetone fractional precipitation albumen.
) enzymolysis of red cartilage acetone fractional precipitation albumen: take red cartilage 60% acetone fractional precipitation albumen and be dissolved in Tris-HCl buffer (0.05mol/L according to solid-liquid ratio 1g:3��5mL, pH7.5��8.5), add trypsin 1.9 �� 10 according to the 2.0��3.0% of 60% acetone fractional precipitation protein by weight4U/g), in 40 DEG C of enzymolysis 3��5h, then in 90 DEG C, the work of 10min enzyme denaturing, enzymolysis solution, in 4 DEG C, the centrifugal 15��25min of 10000��12000r/min, is abandoned residue and is collected supernatant, obtain chondroprotein enzymolysis solution.
) preparation of red chondroprotein anti-oxidation peptide: adopt 3kDa ultrafilter membrane to carry out hyperfiltration treatment above-mentioned enzymolysis solution, collect molecular weight less than 3kDa part, lyophilizing, obtain ultrafiltration zymolyte; By ultrafiltration zymolyte time through resinbed analysis, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) purification, obtain anti-oxidation peptide.
As preferably, red for red (Dasyatisakajei) in described step 1).
As preferably, the detailed process of the resinbed analysis of described step 4), gel filtration chromatography and RP-HPLC purification is:
Resinbed is analysed: above-mentioned ultrafiltration zymolyte is dissolved in distilled water and is made into the solution that concentration is 45��55mg/mL, post is analysed through DEAE-52 resinbed, eluting is carried out with water, 0.1mol/L, 0.5mol/L and 1.0mol/LNaCl solution, flow velocity is 0.6��0.8mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, solution in test tube is merged by peak, compare the DPPH free radical at each peak and the scavenging capacity of hydroxyl radical free radical, select the strongest component lyophilizing of activity, be ion-exchange chromatography zymolyte;
Gel filtration chromatography: above-mentioned ion-exchange chromatography zymolyte is dissolved in distilled water and is made into the solution that concentration is 45��55mg/mL, through polydextran gel SephadexG-15 column chromatography for separation, eluting is carried out with distilled water, flow velocity is 0.6��0.8mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, merges solution in test tube by peak, compares the DPPH free radical at each peak and the scavenging capacity of hydroxyl radical free radical, select the strongest component lyophilizing of activity, be gel chromatography zymolyte;
RP-HPLC purification: above-mentioned gel chromatography zymolyte distilled water is made into the solution of 80��100 �� g/mL, RP-HPLC is utilized to be purified, obtaining 1 high activity anti-oxidation peptide Ile-Glu-Pro-His (IEPH) according to the scavenging capacity of DPPH free radical and hydroxyl radical free radical, it is 494.55Da that ESI-MS measures molecular weight.
Further preferably, described RP-HPLC condition is: sample size 10��15 �� L; Chromatographic column ZorbaxSB-C18(250mm �� 4.6mm, 5 ��m); Mobile phase: water-acetonihile gradient elution (0��32min acetonitrile concentration is at the uniform velocity risen to 50% by 0); Elution speed 0.6 ~ 1.0mL/min; Ultraviolet detection wavelength 280nm.
Compared with prior art, DPPH free radical, hydroxyl radical free radical and ultra-oxygen anion free radical are had good scavenging action by red chondroprotein anti-oxidation peptide provided by the present invention; Meanwhile, Ile-Glu-Pro-His (IEPH) also demonstrates good Lipid peroxidation; Ile-Glu-Pro-His (IEPH) has safe without toxic side effect, antioxidant activity is strong and is prone to advantages such as digesting and assimilating, it is possible to as the additive of medicine, health food and food.
Accompanying drawing explanation
Fig. 1 is the DEAE-52 resinbed analysis figure of the present invention.
Fig. 2 is the polydextran gel SephadexG-15 tomographic map of the present invention.
Fig. 3 polydextran gel SephadexG-15 prepares the RP-HPLC of zymolyte and analyzes.
The mass spectrum of Fig. 4 Ile-Glu-Pro-His (IEPH).
The lipid peroxidation inhibition ability of Fig. 5 Ile-Glu-Pro-His (IEPH).
Detailed description of the invention
Below in conjunction with accompanying drawing embodiment, the present invention is described in further detail.
Embodiment:
The preparation method of red chondroprotein anti-oxidation peptide, preparation technology flow process is as follows: red cartilage " cartilage total protein " cartilage 60% acetone precipitation albumen " trypsin digestion " zymolyte " ultrafiltration " ion-exchange chromatography " gel permeation chromatography " high performance liquid chromatography prepares " anti-oxidation peptide.
) preparation of red cartilage total protein crude extract: weigh Raja porosa cartilage and be cut into fine grained chippings, add appropriate distilled water, in high-speed tissue mashing machine, homogenate is to pasty state, the red cartilage of pasty state is dipped in the 1.0mol/L guanidine hydrochloride solution of 5 times of volumes (containing 0.02mol/LMES and 0.02mol/LEDTA, pH7.0), at 4 DEG C, extracting 48h is stirred. Extracting solution with the centrifugal 20min of 4500r/min, is abandoned residue and is collected supernatant at 4 DEG C; Supernatant continues, at 4 DEG C, the centrifugal 20min of 12000r/min, to take supernatant and remove insoluble impurities with 0.22 ��m of filtering with microporous membrane. Filtrate being loaded in the bag filter that molecular retention amount is 8000, with Tris-HCl(pH7.6) buffer dialyses 48h at 4 DEG C, and in bag filter, solution is red cartilage total protein crude extract.
) preparation of red cartilage acetone fractional precipitation albumen: take red cartilage total protein crude extract, being slowly added to pre-cold acetone to acetone concentration under ice bath is 30%, after standing 5h at-20 DEG C, in 4 DEG C, 12000r/min high speed centrifugation 20min, taking supernatant, adding pre-cold acetone to the final acetone concentration of solution is 60%, it is thus achieved that red cartilage 60% acetone precipitation albumen, lyophilizing, obtains 60% acetone fractional precipitation albumen.
) enzymolysis of red cartilage acetone fractional precipitation albumen: take red cartilage 60% acetone fractional precipitation albumen and be dissolved in Tris-hydrochloride buffer (0.05mol/L according to solid-liquid ratio 1g:4mL, pH8.0), trypsin 1.9 �� 10 is added according to the 2.5% of 60% acetone fractional precipitation protein by weight4U/g), in 40 DEG C of enzymolysis 4h, then in 90 DEG C, the work of 10min enzyme denaturing, enzymolysis solution, in 4 DEG C, the centrifugal 20min of 12000r/min, is abandoned residue and is collected supernatant, obtain chondroprotein enzymolysis solution.
) preparation of red chondroprotein anti-oxidation peptide: adopt 3kDa ultrafilter membrane to carry out hyperfiltration treatment above-mentioned enzymolysis solution, collect molecular weight less than 3kDa part (DP60-I), obtain ultrafiltration enzymolysis solution, by ultrafiltration enzymolysis solution successively through resinbed analysis, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) purification, obtain anti-oxidation peptide.
1. resinbed analysis: DP60-I is dissolved in distilled water and is made into the solution that concentration is 50mg/mL, post is analysed through DEAE-52 resinbed, eluting is carried out with water, 0.1mol/L, 0.5mol/L and 1.0mol/LNaCl solution, flow velocity is 0.6mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, solution in test tube is merged by peak, compare DPPH free radical and the Hydroxyl radical-scavenging ability at each peak, select the strongest component lyophilizing of oxidation resistance, be ion-exchange chromatography zymolyte DP60-3(Fig. 1);
2. gel filtration chromatography: DP60-3 is dissolved in distilled water and is made into the solution that concentration is 50mg/mL, through polydextran gel SephadexG-15 column chromatography for separation, eluting is carried out with distilled water, flow velocity is 0.6��0.8mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, merges solution in test tube by peak, compares DPPH free radical and the Hydroxyl radical-scavenging ability at each peak, select the strongest component lyophilizing of oxidation resistance, be gel chromatography zymolyte DP60-3-1(Fig. 2);
3. RP-HPLC purification: DP60-3-1 distilled water is made into the solution of 80��100 �� g/mL, (RP-HPLC condition is: sample size 15 �� L to utilize RP-HPLC to be purified; Chromatographic column ZorbaxSB-C18(250mm �� 4.6mm, 5 ��m); Mobile phase: water-acetonihile gradient elution (0��32min acetonitrile concentration is at the uniform velocity risen to 50% by 0); Elution speed 0.8mL/min; Ultraviolet detection wavelength 280nm), obtain 1 high activity anti-oxidation peptide DCPE-B(Fig. 3 according to the scavenging capacity of DPPH free radical and hydroxy radical).
4. structure detection: collect DPPH free radical and the highest anti-oxidation peptide DCPE-B of Scavenging activity on hydroxyl free radical, it is simple spike through RP-HPLC detection, utilizing protein/polypeptide sequenator to measure aminoacid sequence is Ile-Glu-Pro-His (IEPH), and it is 494.55Da([M+H that ESI-MS measures molecular weight]+495.96Da) (Fig. 4).
Prepared red chondroprotein anti-oxidation peptide Ile-Glu-Pro-His (IEPH) is carried out free radical scavenging experiment and lipid peroxidation Inhibition test, test result indicate that: Ile-Glu-Pro-His (IEPH) is to DPPH free radical (EC502.42mg/mL), hydroxyl radical free radical (EC500.39mg/mL), ABTS free radical (EC500.11mg/mL) with ultra-oxygen anion free radical (EC500.17mg/mL); Meanwhile, Ile-Glu-Pro-His (IEPH) also demonstrates good Lipid peroxidation (Fig. 5).
Finally, in addition it is also necessary to be only the specific embodiment of the present invention it is noted that listed above. It is clear that the invention is not restricted to above example, it is also possible to there are many deformation. All deformation that those of ordinary skill in the art can directly derive from present disclosure or associate, are all considered as protection scope of the present invention.
SEQUENCELISTING
<110>Oceanography Institute Of Zhejiang
<120>preparation method of red chondroprotein anti-oxidation peptide
<130>zjou-wb-201511-202
<160>1
<170>PatentInversion3.5
<210>1
<211>4
<212>PRT
<213>artificial sequence
<400>1
IleGluProHis
1
Claims (5)
1. the preparation method of red chondroprotein anti-oxidation peptide, it is characterised in that comprise the following steps:
1) preparation of red cartilage total protein crude extract: weigh Raja porosa cartilage and be cut into fine grained chippings, add appropriate distilled water, in high-speed tissue mashing machine, homogenate is to pasty state, the red cartilage of pasty state is dipped in the 1.0mol/L guanidine hydrochloride solution of 4��6 times of volumes, this guanidine hydrochloride solution is 7��8 containing 0.02mol/LMES, 0.02mol/LEDTA and pH value, at 4 DEG C, stirs extracting 36��48h;Extracting solution with the centrifugal 15��25min of 4000��6000r/min, is abandoned residue and is collected supernatant at 4 DEG C; Supernatant continues, at 4 DEG C, the centrifugal 15��25min of 10000��12000r/min, to take supernatant and remove insoluble impurities with 0.22 ��m of filtering with microporous membrane; Filtrate being loaded in the bag filter that molecular retention amount is 8000, dialyse 24��48h with the Tris-HCl buffer that pH value is 7.6 at 4 DEG C, in bag filter, solution is red cartilage total protein crude extract;
2) preparation of red cartilage acetone fractional precipitation albumen: taking red cartilage total protein crude extract, to be slowly added to pre-cold acetone to acetone concentration under ice bath be 30%, after standing 4��6h at-20 DEG C, in 4 DEG C, 10000��12000r/min high speed centrifugation 20min, take supernatant, adding pre-cold acetone to the final acetone concentration of solution is 60%, obtain red cartilage 60% acetone precipitation albumen, lyophilizing, be 60% acetone fractional precipitation albumen;
3) enzymolysis of red cartilage acetone fractional precipitation albumen: take red cartilage 60% acetone fractional precipitation albumen and be dissolved in Tris-HCl buffer according to solid-liquid ratio 1g:3��5mL, this buffer is 0.05mol/L, pH value is 7.5��8.5, adds 1.9 �� 10 according to the 2.0��3.0% of 60% acetone fractional precipitation protein by weight4The trypsin of U/g, in 40 DEG C of enzymolysis 3��5h, then in 90 DEG C, the work of 10min enzyme denaturing, enzymolysis solution, in 4 DEG C, the centrifugal 15��25min of 10000��12000r/min, is abandoned residue and is collected supernatant, obtain chondroprotein enzymolysis solution;
4) preparation of red chondroprotein anti-oxidation peptide: adopt 3kDa ultrafilter membrane to carry out hyperfiltration treatment above-mentioned enzymolysis solution, collects molecular weight less than 3kDa part, lyophilizing, obtains ultrafiltration zymolyte; By ultrafiltration zymolyte time through resinbed analysis, gel filtration chromatography and reversed-phase high-performance liquid chromatography purification, obtain anti-oxidation peptide.
2. preparation method according to claim 1, it is characterised in that red for red i.e. Dasyatisakajei in described step 1).
3. preparation method according to claim 1, it is characterised in that the detailed process of the resinbed analysis of described step 4), gel filtration chromatography and reversed-phase high-performance liquid chromatography purification is:
Resinbed is analysed: above-mentioned ultrafiltration zymolyte is dissolved in distilled water and is made into the solution that concentration is 45��55mg/mL, post is analysed through DEAE-52 resinbed, eluting is carried out with water, 0.1mol/L, 0.5mol/L and 1.0mol/LNaCl solution, flow velocity is 0.6��0.8mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, solution in test tube is merged by peak, compare the DPPH free radical at each peak and the scavenging capacity of hydroxyl radical free radical, select the strongest component lyophilizing of activity, be ion-exchange chromatography zymolyte;
Gel filtration chromatography: above-mentioned ion-exchange chromatography zymolyte is dissolved in distilled water and is made into the solution that concentration is 45��55mg/mL, through polydextran gel SephadexG-15 column chromatography for separation, eluting is carried out with distilled water, flow velocity is 0.6��0.8mL/min, the every 3min of wash solution collects a pipe and detects in 280nm, merges solution in test tube by peak, compares the DPPH free radical at each peak and the scavenging capacity of hydroxyl radical free radical, select the strongest component lyophilizing of activity, be gel chromatography zymolyte;
Reversed-phase high-performance liquid chromatography purification: above-mentioned gel chromatography zymolyte distilled water is made into the solution of 80��100 �� g/mL, reversed-phase high-performance liquid chromatography is utilized to be purified, according to the scavenging capacity of DPPH free radical and hydroxyl radical free radical obtains 1 high activity anti-oxidation peptide Ile-Glu-Pro-His, ESI-MS, to measure molecular weight be 494.55Da.
4. preparation method according to claim 1, it is characterised in that the condition of described reversed-phase high-performance liquid chromatography is: sample size 10��15 �� L; Chromatographic column is specification is 250mm �� 4.6mm, the ZorbaxSB-C of 5 ��m18; Mobile phase is water-acetonihile gradient elution, and 0��32min acetonitrile concentration is at the uniform velocity risen to 50% by 0; Elution speed 0.6 ~ 1.0mL/min; Ultraviolet detection wavelength 280nm.
5. preparation method according to claim 1, it is characterised in that prepared anti-oxidation peptide is Ile-Glu-Pro-His, ESI-MS mensuration molecular weight is 494.55Da.
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007217358A (en) * | 2006-02-17 | 2007-08-30 | Nippon Meat Packers Inc | Anti-oxidizing peptide |
| CN103204904A (en) * | 2013-02-01 | 2013-07-17 | 浙江海洋学院 | Dasyatis akajei chondroprotein polypeptide capable of resisting prostate cancer, and preparation method and application thereof |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007217358A (en) * | 2006-02-17 | 2007-08-30 | Nippon Meat Packers Inc | Anti-oxidizing peptide |
| CN103204904A (en) * | 2013-02-01 | 2013-07-17 | 浙江海洋学院 | Dasyatis akajei chondroprotein polypeptide capable of resisting prostate cancer, and preparation method and application thereof |
Non-Patent Citations (2)
| Title |
|---|
| ZHONGRUI LI等: "Influence of average molecular weight on antioxidant and functional properties of cartilage collagen hydrolysates from Sphyrna lewini, Dasyatis akjei and Raja porosa", 《FOOD RESEARCH INTERNATIONAL》 * |
| 胡发远: "孔鳐软骨多肽及泥蚶多肽的制备及活性研究", 《中国优秀硕士学位论文全文数据库 工程科技I辑》 * |
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