CN105725110A - Method for preparing antioxidant product from scallop skirts - Google Patents
Method for preparing antioxidant product from scallop skirts Download PDFInfo
- Publication number
- CN105725110A CN105725110A CN201610101561.XA CN201610101561A CN105725110A CN 105725110 A CN105725110 A CN 105725110A CN 201610101561 A CN201610101561 A CN 201610101561A CN 105725110 A CN105725110 A CN 105725110A
- Authority
- CN
- China
- Prior art keywords
- scallop body
- scallop
- zymolyte
- oxidation product
- enzymolysis
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 241000237509 Patinopecten sp. Species 0.000 title claims abstract description 102
- 235000020637 scallop Nutrition 0.000 title claims abstract description 102
- 238000000034 method Methods 0.000 title claims abstract description 23
- 230000003078 antioxidant effect Effects 0.000 title abstract description 7
- 239000003963 antioxidant agent Substances 0.000 title abstract description 4
- 238000006243 chemical reaction Methods 0.000 claims abstract description 34
- 108090000145 Bacillolysin Proteins 0.000 claims abstract description 12
- 102000035092 Neutral proteases Human genes 0.000 claims abstract description 12
- 108091005507 Neutral proteases Proteins 0.000 claims abstract description 12
- 238000004108 freeze drying Methods 0.000 claims abstract description 11
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 9
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 9
- 108090000526 Papain Proteins 0.000 claims abstract description 7
- 239000004365 Protease Substances 0.000 claims abstract description 7
- 229940055729 papain Drugs 0.000 claims abstract description 7
- 235000019834 papain Nutrition 0.000 claims abstract description 7
- 239000000047 product Substances 0.000 claims description 45
- 230000003064 anti-oxidating effect Effects 0.000 claims description 42
- 239000008176 lyophilized powder Substances 0.000 claims description 25
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 claims description 12
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 claims description 12
- 239000000758 substrate Substances 0.000 claims description 10
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 claims description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
- 238000012545 processing Methods 0.000 claims description 8
- 239000000243 solution Substances 0.000 claims description 8
- 102000004190 Enzymes Human genes 0.000 claims description 7
- 108090000790 Enzymes Proteins 0.000 claims description 7
- 229940088598 enzyme Drugs 0.000 claims description 7
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 claims description 6
- 238000010298 pulverizing process Methods 0.000 claims description 6
- 239000012460 protein solution Substances 0.000 claims description 5
- 230000003412 degenerative effect Effects 0.000 claims description 4
- 238000001976 enzyme digestion Methods 0.000 claims description 4
- 238000010438 heat treatment Methods 0.000 claims description 4
- 239000006228 supernatant Substances 0.000 claims description 4
- 238000011282 treatment Methods 0.000 claims description 4
- 229930091371 Fructose Natural products 0.000 claims description 3
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 claims description 3
- 239000005715 Fructose Substances 0.000 claims description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 3
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 claims description 3
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 claims description 3
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 3
- 239000008103 glucose Substances 0.000 claims description 3
- 238000005121 nitriding Methods 0.000 claims description 3
- 239000000376 reactant Substances 0.000 claims description 3
- 239000002904 solvent Substances 0.000 claims description 3
- 239000011550 stock solution Substances 0.000 claims description 2
- 238000012986 modification Methods 0.000 abstract description 3
- 230000004048 modification Effects 0.000 abstract description 3
- 239000000843 powder Substances 0.000 abstract 2
- 238000009776 industrial production Methods 0.000 abstract 1
- 230000003647 oxidation Effects 0.000 description 18
- 238000007254 oxidation reaction Methods 0.000 description 18
- -1 DPPH free radical Chemical class 0.000 description 13
- HHEAADYXPMHMCT-UHFFFAOYSA-N dpph Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1[N]N(C=1C=CC=CC=1)C1=CC=CC=C1 HHEAADYXPMHMCT-UHFFFAOYSA-N 0.000 description 9
- 230000007071 enzymatic hydrolysis Effects 0.000 description 6
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 6
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 230000002000 scavenging effect Effects 0.000 description 5
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 239000006227 byproduct Substances 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 125000000548 ribosyl group Chemical group C1([C@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000000205 computational method Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 239000000796 flavoring agent Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 108010005094 Advanced Glycation End Products Proteins 0.000 description 1
- 241001597008 Nomeidae Species 0.000 description 1
- 238000012356 Product development Methods 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000013355 food flavoring agent Nutrition 0.000 description 1
- 230000007760 free radical scavenging Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 235000008935 nutritious Nutrition 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 238000012958 reprocessing Methods 0.000 description 1
- 235000013599 spices Nutrition 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Abstract
The invention discloses a method for preparing an antioxidant product from scallop skirts. The method comprises the steps that the scallop skirts are pretreated, neutral protease and papain are adopted for performing enzymolysis on obtained scallop skirt freeze-dried powder, freeze-drying is performed, and scallop skirt zymolyte is prepared; prepared scallop skirt zymolyte freeze-dried powder is subjected to Maillard reaction modification, and then the antioxidant product is prepared from the scallop skirts. According to the method, protein resources in the scallop skirts are fully utilized, the utilization rate of the scallop skirts is increased, and the added value of the product is increased. The reaction conditions are mild, the reaction process is stable, and the prepared product has high antioxidant activity; the operation process is simple, and the method is suitable for industrial production.
Description
Technical field
The processing method that the present invention relates to a kind of scallop body added-value product, more particularly, it relates to a kind of method utilizing scallop body to prepare anti-oxidation product.
Background technology
Scallop is nutritious, and namely its closed shell flesh obtain " dry scallop " after drying.Scallop body is the by-product in its closed shell flesh course of processing, and protein content is higher, reaches 65% (with dry weight basis), is the very good material preparing enzymolysis protein peptide.At present, scallop body is processed to the goods such as flavouring agent more, and added value of product is not high, it would be highly desirable to develop further.
Summary of the invention
It is an object of the invention to develop the reprocessing technique of a kind of scallop processing byproduct scallop body, improve the utilization rate of by-product in the scallop course of processing, it is to avoid the wasting of resources.Feature according to the rich in protein of scallop body own, utilizes Maillard reaction, develops a kind of method utilizing scallop body to prepare anti-oxidation product, simultaneously, it is ensured that the method has that mild condition, course of reaction be stable, production efficiency high.
For reaching above-mentioned purpose, the invention provides a kind of method utilizing scallop body to prepare anti-oxidation product, comprise the steps:
S1, scallop body pretreatment: take scallop body, clean, carry out degenerative treatments, lyophilizing, pulverizing in 80～100 DEG C of heating in water bath 10～20min, obtain scallop body lyophilized powder；
S2, adopting the one in neutral protease or papain, the scallop body lyophilized powder that step S1 is obtained carries out enzymolysis processing, enzymolysis after terminating immediately in 80～100 DEG C of heating in water bath 5～15min with enzymolysis reaction, prepare scallop body enzymolysis solution；
S3, the scallop body enzymolysis solution that step S2 prepares is cooled to after room temperature in the centrifugal 10～30min of 3000～5000 × g, collects supernatant, lyophilizing, pulverizing, obtain scallop body zymolyte lyophilized powder；
S4, scallop body zymolyte lyophilized powder and reducing sugar that step S3 prepares carrying out Maillard reaction, reaction will react the direct lyophilization of stock solution after terminating, and be the anti-oxidation product utilizing scallop body prepared.
Under optimal way, the concrete operations of enzyme digestion reaction described in step S2 are:
S21, adopt triumphant formula nitriding determination step S1 prepare scallop body lyophilized powder in protein content；
S22, with water for solvent, weigh step S1 prepare scallop body lyophilized powder prepare the scallop body protein solution that concentration of substrate (with proteinometer) is 4g/100mL；
S23, in the step S22 scallop body protein solution prepared, add the one in 2000～3000 (U/g substrate protein) neutral protease or papain, regulate pH to 7.0,45～55 DEG C of enzymolysis 0.5～3h.
Under optimum way, step S23 adopts neutral protease, and enzyme dosage is 3000 (U/g substrate proteins), and enzyme digestion reaction temperature is 50 DEG C, and enzymolysis time is 2h.
Under optimal way, step S4 is:
The scallop body zymolyte lyophilized powder that step S3 prepares is mixed soluble in water with reducing sugar 1:0.3～3 in mass ratio, prepare the mixed liquor of the final concentration of 10mg/ml of scallop body zymolyte, the NaOH solution adopting 1mol/mL regulates described pH of mixed to after 6～9, heats to 75～95 DEG C and reacts 2～12h；After reaction terminates, by reactant liquor lyophilization, it is the anti-oxidation product utilizing scallop body to prepare；
Described reducing sugar is the one in ribose, xylose, glucose, fructose.
Under optimum way, reducing sugar described in step S4 is ribose；Described scallop body zymolyte lyophilized powder and reducing sugar mass ratio 1:2, the described final concentration of 10mg/mL of scallop body zymolyte；The pH of described mixed liquor is 7.0, and reaction temperature is 95 DEG C, and the response time is 12h.
The technological innovation of the present invention is in that:
1, the inventive method makes full use of the protein resource in scallop body, improves scallop body utilization rate as by-product in the scallop course of processing so that it is potential anti-oxidation active substance is fully developed utilization, decreases the waste of resource.
2, the inventive method reaction condition is gentle, and course of reaction is stable, and raw material resources are enriched, and prepare product and have higher antioxidant activity, contains better nutritivity simultaneously and is worth, and the fresh perfume (or spice) of local flavor can be used for developing in numerous food product development as function base material.
3, the operating process that the inventive method relates to is simple, it is not necessary to complicated equipment, and the anti-oxidation product obtained is for removing the IC of DPPH50Value can reach 0.442 ± 0.03mg/ml, the IC of simple zymolyte50Value is anti-oxidation product IC5024.1 times of value, illustrate that scallop body zymolyte oxidation resistance after Maillard reaction significantly improves, are a kind of effective and practical scallop body anti-oxidation product preparation methoies, are suitable for industrialized production.
Accompanying drawing explanation
Fig. 1 is the oxidation resistance comparison diagram utilizing scallop body anti-oxidation product under different reducing sugar；
Fig. 2 is the oxidation resistance comparison diagram utilizing scallop body anti-oxidation product at differential responses temperature；
Fig. 3 is that different peptide sugar is than the lower oxidation resistance comparison diagram utilizing scallop body anti-oxidation product；
Fig. 4 is the oxidation resistance comparison diagram utilizing scallop body anti-oxidation product under different pH values；
Detailed description of the invention
Embodiment 1
S1, take scallop body, in 100 DEG C of water-baths, heat 10min after cleaning carry out degenerative treatments, cooling, lyophilization, pulverizing, obtain scallop body lyophilized powder；
S2, respectively with neutral protease, papain for toolenzyme, enzyme dosage 3000U/g albumen, concentration of substrate (with proteinometer) 4g/100mL, constant pH 7, hydrolysis temperature 50 DEG C enzymatic hydrolysis condition under scallop body lyophilized powder is carried out enzymolysis processing；Enzymolysis time is 0.5h respectively, 1h, 2h, 3h.100 DEG C of water-bath enzyme denaturing 10min after enzymolysis, under 4000 × g, centrifugal 10min, takes supernatant lyophilization and obtains 8 kinds of scallop body zymolyte lyophilized powders；Utilize the 8 kinds of scallop body zymolytes of the chemical determination Scavenging activity to DPPH free radical, with DPPH free radical semi-inhibit rate (IC50) for index screening optimum enzymatic hydrolysis condition, obtain result as shown in table 1.
Protein content in the scallop body lyophilized powder prepared in the embodiment of the present invention adopts triumphant formula nitriding to measure, the protein content recorded is 65% (with dry weight basis), when preparing the scallop body protein solution that concentration of substrate (with proteinometer) is 4g/100mL, the scallop body lyophilized powder suspension of 6.15g/100mL need to be prepared.
S3,8 kinds of scallop body zymolyte lyophilized powders prepared by enzymatic hydrolysis condition described in S2, under the same conditions, carry out Maillard reaction modification respectively, and reducing sugar is ribose, and with water for solvent, the concentration of scallop body zymolyte is 10mg/mL, and the concentration of ribose is 20mg/mL；Every kind of mixed solution is allocated as identical two part, regulates pH to 7 by the NaOH solution of 1mol/mL, after 8, by above-mentioned solution under 95 DEG C of conditions, reacts 12h respectively.
After S4, the reactant liquor lyophilization obtained by S3, obtain 16 kinds of anti-oxidation product utilizing scallop body to prepare altogether.
Utilize that chemical determination step S4 obtains 16 kinds utilize anti-oxidation product that scallop body the prepares Scavenging activity to DPPH free radical, with DPPH free radical semi-inhibit rate (IC50) for index screening optimum enzymatic hydrolysis condition, test result is as shown in table 1.
Semi-inhibit rate (IC50) it is the common counter characterizing material oxidation resistance, this index reflects concentration when antioxidant provides 50% inhibitory action.DPPH free radical semi-inhibit rate (IC50) computational methods be: first measure variable concentrations scallop body zymolyte and the Maillard reaction derivant (anti-oxidation product) Scavenging activity to DPPH free radical thereof, with sample concentration (mg/mL) for abscissa, DPPH clearance rate (%) is vertical coordinate, adopt Excel software to do scatterplot, and do regression equation analysis.By regression equation, calculate DPPH clearance rate when being 50%, the concentration of scallop body zymolyte and anti-oxidation product thereof, it is DPPH free radical semi-inhibit rate (IC50Value).
With DPPH free radical semi-inhibit rate (IC50Value) for index, the more low explanation oxidation resistance of this numerical value is more strong.8 kinds of scallop body zymolytes are after Maillard reaction is modified, and its oxidation resistance is all remarkably reinforced.Integrated comparative, the scallop body zymolyte obtained through neutral protease enzymolysis is after Maillard reaction is modified, it is thus achieved that the oxidation resistance of anti-oxidation product be better than the anti-oxidation product that the zymolyte of papain obtains after Maillard reaction is modified.
For the zymolyte obtained with neutral protease enzymolysis, under different enzymolysis times, the oxidation resistance difference of the anti-oxidation product of its acquisition is also little, consider from the angle of enzymolysis efficiency, determine that enzymolysis optimal conditions is: adopt neutral protease, enzyme dosage is 3000 (U/g substrate proteins), and temperature is 50 DEG C, and enzymolysis time is 2h.
Table 1
Embodiment 2
S1, take scallop body, in 100 DEG C of water-baths, heat 10min after cleaning carry out degenerative treatments, cooling, lyophilization, pulverizing, obtain scallop body lyophilized powder；
S2, under optimum way, carry out enzymolysis, adopt neutral protease, enzyme dosage 3000U/g albumen, concentration of substrate (with proteinometer) 4g/100mL, constant pH 7, hydrolysis temperature 50 DEG C enzymatic hydrolysis condition under scallop body lyophilized powder carried out enzymolysis processing, enzymolysis time 2h.100 DEG C of water-bath enzyme denaturing 10min after enzymolysis, under 4000 × g, centrifugal 10min, takes supernatant lyophilization and obtains scallop body zymolyte lyophilized powder；
S3, under the optimum enzymatic hydrolysis condition described in S2 preparation zymolyte carry out Maillard reaction modification, reducing sugar is ribose, xylose, glucose, fructose, the mass ratio of scallop body zymolyte and reducing sugar is 1:0.3～3, reaction mixture pH value is 6～9, reaction temperature is 75～95 DEG C, and the response time is 0～12h；Concrete reaction condition is in Table 2, and under different condition, the oxidation resistance comparing result of scallop body anti-oxidation product is shown in Fig. 1～4.
Table 2
Utilize the anti-oxidation product obtained in the chemical determination S3 Scavenging activity to DPPH free radical, with DPPH free radical scavenging activity for index screening optimum reaction condition (see Fig. 1～4).As shown in Figure 1, with ribose for reducing sugar, the time is more long, and the oxidation resistance of the anti-oxidation product prepared is more strong；As shown in Figure 2, temperature is more high, and the oxidation resistance of the anti-oxidation product prepared is more strong；From the figure 3, it may be seen that when peptide sugar is stronger than the product oxidation resistance when 1:2 or 1:3；As shown in Figure 4, pH is little on the impact of its oxidation resistance.
The optimal conditions determining scallop body zymolyte Maillard reaction is: reducing sugar is ribose, temperature 95 DEG C, pH7.0, time 12h, and the concentration of scallop body zymolyte is 10mg/mL, and the concentration of ribose is 20mg/mL, and peptide sugar is than for 1:2.
S4, under step S3 different condition preparation scallop body zymolyte maillard reaction product carry out lyophilization, it is the anti-oxidation product utilizing scallop body to prepare, goods are evaluated its antioxidant activity further with ESR method, and with synthetized oxidation preventive agent 2,6-di-tert-butyl-4-methy phenol (BHT) for positive control.
Table 3 is the anti-oxidation product Scavenging activity to DPPH free radical that the scallop body zymolyte utilizing ESR method to measure prepares.DPPH free radical semi-inhibit rate (IC50Value) computational methods: according to ESR collection of illustrative plates calculate DPPH clearance rate (%), respectively with scallop body zymolyte, prepared anti-oxidation product, BHT (mg/mL) concentration for abscissa, DPPH clearance rate (%) is vertical coordinate, Excel software is adopted to do scatterplot, and do regression equation analysis, calculate DPPH clearance rate when being 50%, the concentration of scallop body zymolyte or its anti-oxidation product prepared, it is DPPH free radical semi-inhibit rate (IC50Value).With DPPH free radical semi-inhibit rate (IC50Value) for index, the more low explanation oxidation resistance of this numerical value is more strong.
Table 3
The anti-oxidation product prepared under the optimal conditions of the above-mentioned steps S3 IC to DPPH free radical50Value is 0.442 ± 0.03mg/ml, the IC of zymolyte50Value is anti-oxidation product IC5024.1 times of value, compare with positive control 2,6-di-tert-butyl-4-methy phenol (BHT), its oxidation resistance one order of magnitude of difference.
Step S3 Maillard reaction reducing sugar be ribose, scallop body zymolyte concentration be 10mg/mL, the concentration of ribose is 20mg/mL, peptide sugar than for 1:2, response time and acid-base value different when:
Reaction mixture pH value is 7, and reaction temperature is 95 DEG C, and when the response time is 6h, prepared anti-oxidation product removes the IC of DPPH free radical50Value is 0.685 ± 0.001mg/ml, the IC of zymolyte50Value is anti-oxidation product IC5015.4 times of value；
Reaction mixture pH value is 8, and in the response time respectively 6 and during 12h, prepared anti-oxidation product removes the IC of DPPH free radical50Value respectively 0.726 ± 0.004mg/ml and 0.655 ± 0.003mg/ml, the IC of zymolyte50Value is anti-oxidation product IC respectively5014.6 and 16.1 times of value.
The above; it is only the present invention preferably detailed description of the invention; but protection scope of the present invention is not limited thereto; any those familiar with the art is in the technical scope of present disclosure; it is equal to replacement according to technical scheme and inventive concept thereof or is changed, all should be encompassed within protection scope of the present invention.
Claims (5)
1. one kind utilizes the method that scallop body prepares anti-oxidation product, it is characterised in that comprise the steps:
S1, scallop body pretreatment: take scallop body, clean, carry out degenerative treatments, lyophilizing, pulverizing in 80～100 DEG C of heating in water bath 10～20min, obtain scallop body lyophilized powder；
S2, adopting the one in neutral protease or papain, the scallop body lyophilized powder that step S1 is obtained carries out enzymolysis processing, enzymolysis after terminating immediately in 80～100 DEG C of heating in water bath 5～15min with enzymolysis reaction, prepare scallop body enzymolysis solution；
S3, the scallop body enzymolysis solution that step S2 prepares is cooled to after room temperature in the centrifugal 10～30min of 3000～5000 × g, collects supernatant, lyophilizing, pulverizing, obtain scallop body zymolyte lyophilized powder；
S4, scallop body zymolyte lyophilized powder and reducing sugar that step S3 prepares carrying out Maillard reaction, reaction will react the direct lyophilization of stock solution after terminating, and be the anti-oxidation product utilizing scallop body prepared.
2. utilize the method that scallop body prepares anti-oxidation product according to claim 1, it is characterised in that the concrete operations of enzyme digestion reaction described in step S2 are:
S21, adopt triumphant formula nitriding determination step S1 prepare scallop body lyophilized powder in protein content；
S22, with water for solvent, weigh step S1 prepare scallop body lyophilized powder prepare the scallop body protein solution that concentration of substrate (with proteinometer) is 4g/100mL；
S23, in the step S22 scallop body protein solution prepared, add the one in 2000～3000 (U/g substrate protein) neutral protease or papain, regulate pH to 7.0,45～55 DEG C of enzymolysis 0.5～3h.
3. stating the method utilizing scallop body to prepare anti-oxidation product according to claim 2, it is characterised in that step S23 adopts neutral protease, enzyme dosage is 3000 (U/g substrate proteins), and enzyme digestion reaction temperature is 50 DEG C, and enzymolysis time is 2h.
4. utilize the method that scallop body prepares anti-oxidation product according to claim 1, it is characterised in that step S4 is:
The scallop body zymolyte lyophilized powder that step S3 prepares is mixed soluble in water with reducing sugar 1:0.3～3 in mass ratio, prepare the mixed liquor of the final concentration of 10mg/ml of scallop body zymolyte, the NaOH solution adopting 1mol/mL regulates described pH of mixed to after 6～9, heats to 75～95 DEG C and reacts 2～12h；After reaction terminates, by reactant liquor lyophilization, it is the anti-oxidation product utilizing scallop body to prepare；
Described reducing sugar is the one in ribose, xylose, glucose, fructose.
5. utilize the method that scallop body prepares anti-oxidation product according to claim 4, it is characterised in that reducing sugar described in step S4 is ribose；Described scallop body zymolyte lyophilized powder and reducing sugar mass ratio 1:2, the described final concentration of 10mg/mL of scallop body zymolyte；The pH of described mixed liquor is 7.0, and reaction temperature is 95 DEG C, and the response time is 12h.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610101561.XA CN105725110A (en) | 2016-02-25 | 2016-02-25 | Method for preparing antioxidant product from scallop skirts |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610101561.XA CN105725110A (en) | 2016-02-25 | 2016-02-25 | Method for preparing antioxidant product from scallop skirts |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN105725110A true CN105725110A (en) | 2016-07-06 |
Family
ID=56248348
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201610101561.XA Pending CN105725110A (en) | 2016-02-25 | 2016-02-25 | Method for preparing antioxidant product from scallop skirts |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN105725110A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107125693A (en) * | 2017-04-28 | 2017-09-05 | 大连工业大学 | A kind of method that utilization Patinopecten yessoensis gonad prepares feature flavor base material |
| CN110754638A (en) * | 2019-10-24 | 2020-02-07 | 大连工业大学 | Preparation method of pre-cooked Fotiaoqiang frozen bag |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102090609A (en) * | 2010-09-06 | 2011-06-15 | 山东好当家海洋发展股份有限公司 | Preparation method of scallop seasoning essence |
| CN102228218A (en) * | 2011-05-27 | 2011-11-02 | 昆明理工大学 | Anti-oxygenation maillard flavor peptides and method for preparing same |
-
2016
- 2016-02-25 CN CN201610101561.XA patent/CN105725110A/en active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102090609A (en) * | 2010-09-06 | 2011-06-15 | 山东好当家海洋发展股份有限公司 | Preparation method of scallop seasoning essence |
| CN102228218A (en) * | 2011-05-27 | 2011-11-02 | 昆明理工大学 | Anti-oxygenation maillard flavor peptides and method for preparing same |
Non-Patent Citations (6)
| Title |
|---|
| 乔路等: "美拉德反应制备鲍鱼脏器肽呈味基料及其抗氧化活性研究", 《大连工业大学学报》 * |
| 俞良莉等: "《食品安全化学》", 31 October 2014, 上海交通大学出版社 * |
| 李彩等: "回归正交旋转法优化制备扇贝裙边抗氧化肽", 《中国食品学报》 * |
| 石燕等: "美拉德反应修饰法制备珍珠蚌抗氧化肽", 《食品与发酵工业》 * |
| 肖军霞等: "牡蛎酶解液的美拉德反应及抗氧化活性研究", 《食品科技》 * |
| 赵谋明等: "木糖-草鱼肽美拉德反应产物的抗氧化性", 《农业工程学报》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107125693A (en) * | 2017-04-28 | 2017-09-05 | 大连工业大学 | A kind of method that utilization Patinopecten yessoensis gonad prepares feature flavor base material |
| CN110754638A (en) * | 2019-10-24 | 2020-02-07 | 大连工业大学 | Preparation method of pre-cooked Fotiaoqiang frozen bag |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN101156645A (en) | A wheat gluten proteolysis matter and method for making same as well as its usage | |
| CN107164447A (en) | A kind of method that utilization cod processing accessory substance prepares anti-oxidation peptide | |
| CN110101034A (en) | The method that a kind of nanometer of high calcium fishbone dust strengthens minced fish gel characteristic | |
| CN112869107A (en) | Method for preparing sauce-flavor fresh base material by using high-temperature peanut cake meal | |
| CN105725110A (en) | Method for preparing antioxidant product from scallop skirts | |
| Zhang et al. | Production and in vitro gastrointestinal digestion of antioxidant peptides from enzymatic hydrolysates of sweet potato protein affected by pretreatment | |
| CN108003219A (en) | A kind of can improve cracks rice protein extracting ratio and carries out the method for glycosylation modification to it | |
| CN108294280A (en) | A kind of graininess beef flavor and preparation method thereof | |
| CN110923285B (en) | Bovine bone peptide and preparation process thereof | |
| CN105707729A (en) | Technology for preparing deer bone meal | |
| CN106749634B (en) | Porcine hemoglobin glycopeptide with antioxidant activity and preparation method and application thereof | |
| Rai et al. | Utilization of tannery fleshings: Optimization of conditions for fermenting delimed tannery fleshings using Enterococcus faecium HAB01 by response surface methodology | |
| CN106117383B (en) | Utilize the method for Patinopecten yessoensis processing byproduct production oligopeptide and glycosaminoglycan | |
| CN105624246A (en) | Preparing method for stichopus japonicus intestine oligopeptide derivative with high oxidation resistance | |
| CN106804873A (en) | A kind of preparation technology of gel soybean protein isolate high | |
| CN105580976A (en) | Method for improving rice protein solubility through combined use of alkaline method and electron beam irradiation | |
| Yang et al. | Effect of pretreatments on hydrolysis efficiency and antioxidative activity of hydrolysates produced from bighead carp (Aristichthys nobilis) | |
| CN107333898A (en) | A kind of free from beany flavor solid Instant Drinks soy protein products and preparation method thereof | |
| CN105200107B (en) | The extracting method of Onchidium struma muscle crude protein | |
| CN105177095A (en) | Method for efficiently preparing antioxidative bioactive peptides of sea cucumbers | |
| CN105211969A (en) | A kind of cepe composite instant ox bone soup stock and preparation method thereof | |
| CN106376864A (en) | Osmund drying method | |
| CN108277080A (en) | A kind of method that enzymatic isolation method prepares soybean oil | |
| Yu et al. | A new multistage counter current extraction method of removing fluoride from defatted Antarctic krill powder | |
| Rai et al. | Optimization of acid hydrolysis conditions of delimed tannery fleshings by response surface method |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20160706 |
|
| RJ01 | Rejection of invention patent application after publication |