CN105254737B - 鱼鳔胶原抗氧化抗疲劳蛋白肽 - Google Patents
鱼鳔胶原抗氧化抗疲劳蛋白肽 Download PDFInfo
- Publication number
- CN105254737B CN105254737B CN201510758952.4A CN201510758952A CN105254737B CN 105254737 B CN105254737 B CN 105254737B CN 201510758952 A CN201510758952 A CN 201510758952A CN 105254737 B CN105254737 B CN 105254737B
- Authority
- CN
- China
- Prior art keywords
- gly
- pro
- protein peptide
- fatigue
- swim bladder
- 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.)
- Active
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 31
- 102000008186 Collagen Human genes 0.000 title claims abstract description 20
- 108010035532 Collagen Proteins 0.000 title claims abstract description 20
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 20
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 20
- 229920001436 collagen Polymers 0.000 title claims abstract description 19
- 230000002929 anti-fatigue Effects 0.000 title claims abstract description 14
- 210000004712 air sac Anatomy 0.000 title claims abstract description 13
- 230000003064 anti-oxidating effect Effects 0.000 title abstract description 7
- 230000003078 antioxidant effect Effects 0.000 claims abstract description 9
- 239000003963 antioxidant agent Substances 0.000 claims abstract description 5
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 2
- 230000000694 effects Effects 0.000 abstract description 19
- 231100000331 toxic Toxicity 0.000 abstract description 2
- 230000002588 toxic effect Effects 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 15
- 238000010828 elution Methods 0.000 description 11
- 229920002527 Glycogen Polymers 0.000 description 10
- 229940096919 glycogen Drugs 0.000 description 10
- 150000003254 radicals Chemical class 0.000 description 9
- WSMYVTOQOOLQHP-UHFFFAOYSA-N Malondialdehyde Chemical compound O=CCC=O WSMYVTOQOOLQHP-UHFFFAOYSA-N 0.000 description 8
- 210000004185 liver Anatomy 0.000 description 8
- 229940118019 malondialdehyde Drugs 0.000 description 8
- 241000251468 Actinopterygii Species 0.000 description 7
- 241000699670 Mus sp. Species 0.000 description 7
- 230000009182 swimming Effects 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 102000016938 Catalase Human genes 0.000 description 6
- 108010053835 Catalase Proteins 0.000 description 6
- 238000011161 development Methods 0.000 description 6
- 230000018109 developmental process Effects 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 5
- 102000019197 Superoxide Dismutase Human genes 0.000 description 4
- 108010012715 Superoxide dismutase Proteins 0.000 description 4
- 230000001965 increasing effect Effects 0.000 description 4
- 210000003205 muscle Anatomy 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 210000000988 bone and bone Anatomy 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 238000004108 freeze drying Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- -1 superoxide anion free radical Chemical class 0.000 description 3
- DTQVDTLACAAQTR-UHFFFAOYSA-N trifluoroacetic acid Substances OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 241001596950 Larimichthys crocea Species 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 230000032683 aging Effects 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 238000005842 biochemical reaction Methods 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 235000021190 leftovers Nutrition 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 210000003463 organelle Anatomy 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 230000004792 oxidative damage Effects 0.000 description 2
- 230000036542 oxidative stress Effects 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- WNXJCQJNRYHLIO-GEMLJDPKSA-N (2s)-2-amino-5-[[(2r)-1-(carboxymethylamino)-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid;hydrate Chemical compound O.OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O WNXJCQJNRYHLIO-GEMLJDPKSA-N 0.000 description 1
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 description 1
- 208000031295 Animal disease Diseases 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 231100000277 DNA damage Toxicity 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108010053070 Glutathione Disulfide Proteins 0.000 description 1
- 102000006587 Glutathione peroxidase Human genes 0.000 description 1
- 108700016172 Glutathione peroxidases Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 1
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- PBCJIPOGFJYBJE-UHFFFAOYSA-N acetonitrile;hydrate Chemical group O.CC#N PBCJIPOGFJYBJE-UHFFFAOYSA-N 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 238000009360 aquaculture Methods 0.000 description 1
- 244000144974 aquaculture Species 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000002032 cellular defenses Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 238000005238 degreasing Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 230000037080 exercise endurance Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000001819 mass spectrum Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 210000000663 muscle cell Anatomy 0.000 description 1
- 230000008789 oxidative DNA damage Effects 0.000 description 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- QEVHRUUCFGRFIF-MDEJGZGSSA-N reserpine Chemical compound O([C@H]1[C@@H]([C@H]([C@H]2C[C@@H]3C4=C(C5=CC=C(OC)C=C5N4)CCN3C[C@H]2C1)C(=O)OC)OC)C(=O)C1=CC(OC)=C(OC)C(OC)=C1 QEVHRUUCFGRFIF-MDEJGZGSSA-N 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 210000002435 tendon Anatomy 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 238000000825 ultraviolet detection Methods 0.000 description 1
- 210000001835 viscera Anatomy 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/461—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
本发明涉及一种鱼鳔胶原抗氧化抗疲劳蛋白肽,该鱼鳔胶原抗氧化抗疲劳蛋白肽的氨基酸序列为:Gly‑Glu‑Pro‑Gly‑Pro‑Met‑Gly‑Leu‑Ala‑Gly‑Pro‑Leu‑Gly‑Pro‑Ala‑Gly‑Gly‑Ser‑Tyr‑Glu‑Ser‑Lys‑Pro‑Asn‑His,其分子量为6719.5718Da。该蛋白肽具有安全无毒副作用和抗氧化抗疲劳活性强等优点。
Description
技术领域
本发明涉及一种从水生生物提取的多肽,尤其涉及一种鱼鳔胶原抗氧化抗疲劳蛋白肽。
背景技术
自由基是机体许多生化反应的中间产物,正常情况下,其产生和清除处于平衡状态。但是,当这一平衡被打破时,自由基会使机体处于氧化压力之下,通过攻击生命大分子物质及各种细胞器,造成机体在分子、细胞及组织器官水平的各种损伤,加速机体的衰老、疲劳并诱发各种疾病。
根据自由基理论,人体疲劳的产生和体内自由基生成相关,因而具有抗氧化活性的物质存在潜在的抗疲劳活性。
天然的生物活性物质相对于市售的合成剂,具有健康安全的优势,因此,开发海洋生物活性物质具有重要意义。
胶原蛋白主要存在于动物的骨、腱、软骨和皮肤等结缔组织中,是结缔组织中胶原蛋白纤维的蛋白质。胶原蛋白在发展历史过程中,其重要的材料来源一直是陆生动物猪和牛,因为它们具有来源丰富的皮和骨。虽然,人们早已了解了鱼胶原蛋白,但遗憾的是,未能将其作为工业上应用的重要材料,这主要是由于水产捕捞来源不稳定,缺乏规模。近年来,环境等诸多因素引发了陆生动物疾病的产生,如疯牛病等,陆生动物蛋白质的安全性受到质疑;而水产养殖和水产品加工业有了很大的发展,鱼皮、鱼鳞、鱼骨和鱼内脏等鱼类加工下脚料的来源日趋稳定,且具有安全性。因而,对鱼类胶原蛋白的应用与开发已经成为人们关注的热点。然而,胶原蛋白独特的三螺旋结构是非常稳定的,加热时间短和加热温度一般时都难以使其分解,因而不容易被消化吸收。而胶原蛋白水解而得的胶原蛋白肽却能弥补这一缺陷,其分子量小,易于身体吸收。国内外的研究已经表明,水产胶原蛋白肽具有多种功能,包括抗氧化、抗疲劳、抑制血管紧张素转化酶、提高免疫力、抗衰老和抗肿瘤等,并且以其具有的高度生物安全性,可广泛应用于食品、化妆品及医药制备等领域,开发前景非常广阔。
鱼鳔作为渔业加工下脚料,常被废弃或作为简单的加工材料而得不到充分的利用。目前,对于鱼鳔蛋白肽的制备及其活性的相关研究甚少,因此,以养殖大黄鱼鱼鳔为原料制备多肽并研究其抗氧化与抗疲劳活性,为海洋药物和保健食品开发提供理论和实验依据。
发明内容
本发明的目的在于提供一种鱼鳔胶原抗氧化抗疲劳蛋白肽,该蛋白肽具有抗氧化、抗疲劳的特性。
本发明为解决上述技术问题所采取的技术方案为:一种鱼鳔胶原抗氧化抗疲劳蛋白肽,该鱼鳔胶原抗氧化抗疲劳蛋白肽的氨基酸序列为Gly-Glu-Pro-Gly-Pro-Met-Gly-Leu-Ala-Gly-Pro-Leu-Gly-Pro-Ala-Gly-Gly-Ser-Tyr-Glu-Ser-Lys-P ro-Asn-His(GEPGPMGLAGPLGPAGGSYESKPNH),其分子量为6719.5718Da。该蛋白肽具有安全无毒副作用和抗氧化抗疲劳活性强等优点。
附图说明
图1是本发明的蛋白肽分子量测定质谱图;
图2是本发明的蛋白肽高效液相色谱C18柱洗脱峰整体洗脱图;
图3是本发明的蛋白肽高效液相色谱C18柱洗脱峰局部洗脱图。
具体实施方式
以下结合附图实施例对本发明作进一步详细描述。
实施例:养殖大黄鱼鱼鳔为原料制备多肽并研究其抗氧化与抗疲劳活性,为海洋药物和保健食品开发提供理论和实验依据。鱼鳔胶原蛋白多功能肽的制备方法,其包括以下步骤:
1)清洗步骤:选取鱼鳔用流动水彻底清洗,剪成小块儿(0.5×0.5cm)。用0.1MNaOH以1:10(w/v),每4h更换一次溶剂,然后用冷蒸馏水洗至中性,可除去非胶原蛋白等杂蛋白;为了脱脂,接着用10%正丁醇以1:10(w/v)的比例浸泡12h,每3h更换一次溶剂,然后用10倍体积的冷蒸馏水冲洗;在浸泡于85%左右的乙醇中12h,每3h更换一次溶剂,最后用冷蒸馏水冲洗。将预处理好的鱼鳔进行匀浆,备用;
2)酶解步骤:以包含动物、植物及微生物蛋白酶在内的4种商业化蛋白酶(木瓜酶、胰蛋白酶、胃蛋白酶及碱性蛋白酶),分别在其最适条件下酶解匀浆后的鱼鳔,酶解时间均为6h,加酶量均为鱼鳔匀浆质量的2%,料液比为1:3;
3)纯化步骤:上述步骤处理得到的组分浓缩、冷冻干燥后,通过Sephadex G-25层析柱(2.6cm×60cm)进一步分离纯化,样品浓度为25mg/mL,上样量为2mL,用去离子水洗脱,洗脱速度为1.5mL/min,于紫外分光光度计280nm下检测,收集各洗脱峰,浓缩后冷冻干燥,检测各洗脱组分的抗氧化活并收集活性较高的洗脱峰进行浓缩,冷冻干燥,以0.1%TFA去离子水配制1mg/mL样品溶液,过0.22μm微孔滤膜,利用RP-HPLC进一步分离纯化,色谱分析条件为:进样量,20μL;色谱柱类型,C18 Hypersil BDS(250mm×4.6mm,5μm);柱温,30;℃流动相为乙腈-水溶液(含有0.1mL/100mL的三氟乙酸),采用梯度洗脱,在50min洗脱时间内乙腈浓度由0%线性递增至100%;洗脱流速,1.0mL/min;紫外检测波长设定280nm。同样收集各洗脱峰后,浓缩并冷冻干燥,经活性筛选出抗氧化活性最强的组分作为目标肽氨基酸序列为:Gly-Glu-Pro-Gly-Pro-Met-Gly-Leu-Ala-Gly-Pro-Leu-Gly-Pro-Ala-Gly-Gly-Ser-Tyr-Glu-Ser-Lys-P ro-Asn-His(GEPGPMGLAGPLGPAGGSYESKPNH)。
自由基是机体许多重要的生化反应的中间代谢产物,正常状况下,其产生和清除处于动态平衡。然而,自由基是有效的防御系统,如果机体不能维持这一动态平衡,则会使自己处于氧化压力状态下,自由基通过攻击机体大分子物质和细胞器,对机体造成损伤。然而,肌肉细胞含有复杂的内源性细胞防御机制以清除氧自由基(如谷胱甘肽过氧化物酶(GSH-Px)、超氧化物歧化酶(SOD)、过氧化氢酶(CAT)等),对机体由运动引发的氧化损伤和DNA损伤具有一定的保护作用。GSH-Px可加速H2O2和GSH的反应,并将它们转化为水和氧化性谷胱甘肽;SOD可以清除超氧阴离子自由基;CAT可以降解羟自由基。
表1本发明蛋白肽(SBP-Ⅲ-3)对小鼠负重游泳时间的影响
组别 | 空白对照组 | 低剂量组 | 中剂量组 | 高剂量组 |
游泳时间(min) | 16.1±1.46 | 25.43±1.91* | 28.86±1.01** | 33.41±5.40** |
注:与对照组比较*P<0.05,**P<0.01;与低剂量组比较aP<0.05,bP<0.01。
评价剧烈运动能力的又一重要指标是能量以糖原形式储存的能力。运动所需能量首先来源于糖原的分解,然后来自肌肉和肝脏中的糖原流通。运动中,当肌糖原减少时,肝糖原含量的降低则成为运动耐力的主要限制因素。因此,增加肝糖原和肌糖原储备有利于增强耐力和运动能力。各剂量组小鼠的肝糖原水平明显高于对照组,并且高剂量组显著高于低剂量组(P<0.05或P<0.01)。剂量组SBP-HG和SBP-MG小鼠的肌糖原水平明显高于对照组(P<0.01)。此结果表明,纯化肽可通过维持体内糖原含量为机体储备能量而达到抗疲劳的效果。
表2本发明蛋白肽(SBP-Ⅲ-3)对小鼠抗氧化酶活力的影响
组别 | 空白对照组 | 低剂量组 | 中剂量组 | 高剂量组 |
T-SOD(U/mg port) | 68.82±6.17 | 71.74±2.52 | 79.63±7.40* | 99.24±4.38**<sup>b</sup> |
GSH-Px(活力单位) | 43.22±4.09 | 71.89±2.34 | 102.05±5.78** | 147.16±12.80**<sup>b</sup> |
CAT(U/mg port) | 186.14±2.26 | 325.27±1.52* | 349.75±4.09* | 483.00±5.87**<sup>a</sup> |
注:与对照组比较*P<0.05,**P<0.01;与低剂量组比较aP<0.05,bP<0.01。
实验通过测定SOD、GSH-Px和CAT的活性以评价纯化肽SBP-Ⅲ-3的抗氧化活性。结果如表2所示与对照组相比,剂量组SBP-HG和SBP-MG小鼠体内的T-SOD活性分别增加了44.2%和15.7%,具有差异显著性,然而低剂量组SBP-LG则增加了4.2%,与对照组并无显著性差异(P<0.05)。另外,剂量组SBP-HG和SBP-MG之间也有显著差异性(P<0.01)。GSH-Px和CAT的活性与T-SOD具有相同趋势。丙二醛(MDA)是一种脂质过氧化物,可以反映机体自由基的含量。本实验还检测了小鼠肝脏和血浆中的MDA含量。结果如表3所示,三个剂量组小鼠的MDA水平均低于对照组水平,且高、中剂量组小鼠的肝脏中MDA含量均显著高于对照组(P<0.05或P<0.01)。以上研究结果表明,该纯化肽可能通过控制自由基的积累以保护机体不受氧化损伤,从而具有抗疲劳的效果。
表3本发明蛋白肽(SBP-Ⅲ-3)对小鼠血浆和肝脏中MDA含量的影响
组别 | 肝脏中MDA(nmol/mL) | 血浆中MDA(nmol/mL) |
NCG | 2.39±0.55 | 19.92±2.87 |
SBP-LG | 1.72±0.25** | 11.75±2.62** |
SBP-MG | 1.23±0.31**<sup>a</sup> | 9.97±1.31** |
SBP-HG | 1.11±0.23**<sup>b</sup> | 9.50±0.55** |
注:与对照组比较*P<0.05,**P<0.01;与低剂量组SBP-LG相比aP<0.05,bP<0.01。
尽管已结合优选的实施例描述了本发明,然其并非用以限定本发明,任何本领域技术人员,在不脱离本发明的精神和范围的情况下,能够对在这里列出的主题实施各种改变、同等物的置换和修改,因此本发明的保护范围当视所提出的权利要求限定的范围为准。
Claims (1)
1.一种鱼鳔胶原抗氧化抗疲劳蛋白肽,其特征该鱼鳔胶原抗氧化抗疲劳蛋白肽的氨基酸序列为:
Gly-Glu-Pro-Gly-Pro-Met-Gly-Leu-Ala-Gly-Pro-Leu-Gly-Pro-Ala-Gly-Gly-Ser-Tyr-Glu-Ser-Lys-Pro-Asn-His,其分子量为6719.5718Da。
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201510758952.4A CN105254737B (zh) | 2015-11-10 | 2015-11-10 | 鱼鳔胶原抗氧化抗疲劳蛋白肽 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201510758952.4A CN105254737B (zh) | 2015-11-10 | 2015-11-10 | 鱼鳔胶原抗氧化抗疲劳蛋白肽 |
Publications (2)
Publication Number | Publication Date |
---|---|
CN105254737A CN105254737A (zh) | 2016-01-20 |
CN105254737B true CN105254737B (zh) | 2020-10-30 |
Family
ID=55094714
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201510758952.4A Active CN105254737B (zh) | 2015-11-10 | 2015-11-10 | 鱼鳔胶原抗氧化抗疲劳蛋白肽 |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN105254737B (zh) |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN106338598A (zh) * | 2016-08-31 | 2017-01-18 | 中国科学院烟台海岸带研究所 | 一种鱼胶原蛋白抗衰老用量的筛选方法 |
CN109295140B (zh) * | 2018-10-22 | 2022-01-18 | 浙江海洋大学 | 一种日本黄姑鱼鱼鳔胶原蛋白源二肽基肽酶-iv抑制肽的制备方法 |
CN112899336A (zh) * | 2021-04-13 | 2021-06-04 | 海南三元星生物科技股份有限公司 | 一种鱼鳔胶原蛋白的提取方法 |
CN113444759A (zh) * | 2021-07-23 | 2021-09-28 | 余凤杰 | 一种乙醇脱氢酶激活肽及其制备方法 |
CN114158621B (zh) * | 2021-12-10 | 2024-03-26 | 宁夏九宝生态农业科技发展有限公司 | 一种枸杞果油和核桃油的组合物及其应用 |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2012160575A2 (en) * | 2011-05-18 | 2012-11-29 | GADRE, Arjun | Method of producing gelatin from fish |
CN102363800B (zh) * | 2011-11-16 | 2014-01-01 | 海南大学 | 一种超声波酶解鱼鳔制备抗氧化寡肽的方法 |
CN103451258B (zh) * | 2013-06-19 | 2015-04-22 | 浙江海洋学院 | 具有高抗疲劳活性的梅鱼鱼鳔胶原蛋白的制备工艺 |
CN103992385B (zh) * | 2014-05-22 | 2017-05-10 | 浙江海洋学院 | 一种大黄鱼鱼鳔抗氧化胶原肽及其制备方法和用途 |
-
2015
- 2015-11-10 CN CN201510758952.4A patent/CN105254737B/zh active Active
Also Published As
Publication number | Publication date |
---|---|
CN105254737A (zh) | 2016-01-20 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN105219827B (zh) | 鱼鳔胶原蛋白多功能肽的制备方法 | |
CN105254737B (zh) | 鱼鳔胶原抗氧化抗疲劳蛋白肽 | |
Tadesse et al. | Production and processing of antioxidant bioactive peptides: A driving force for the functional food market | |
Pezeshk et al. | Fractionation of protein hydrolysates of fish waste using membrane ultrafiltration: investigation of antibacterial and antioxidant activities | |
Thirukumaran et al. | Resource recovery from fish waste: Prospects and the usage of intensified extraction technologies | |
He et al. | Ten new pentapeptides from protein hydrolysate of miiuy croaker (Miichthys miiuy) muscle: Preparation, identification, and antioxidant activity evaluation | |
Duarte et al. | Bovine blood components: fractionation, composition, and nutritive value | |
Udenigwe et al. | Ribulose-1, 5-bisphosphate carboxylase as a sustainable and promising plant source of bioactive peptides for food applications | |
Najafian et al. | A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications | |
CN105410945B (zh) | 鱼鳔胶原蛋白肽的用途 | |
Dong et al. | Selenium accumulation in protein fractions of Tenebrio molitor larvae and the antioxidant and immunoregulatory activity of protein hydrolysates | |
CN110606869B (zh) | 一种促皮肤愈合肽oa-gp11及其制备方法与应用 | |
Espinales et al. | Collagen, protein hydrolysates and chitin from by-products of fish and shellfish: An overview | |
CN110606872A (zh) | 一种促皮肤创伤修复的抗氧化多肽oa-gl17及其制备方法与应用 | |
Doungapai et al. | UV-B protective and antioxidant activities of protein hydrolysate from sea cucumber (Holothuria scabra) using enzymatic hydrolysis | |
CN110590912A (zh) | 一种新型抗氧化活性多肽oa-vi12及其制备方法与应用 | |
Hernández-Ruiz et al. | Collagen peptide fractions from tilapia (Oreochromis aureus Steindachner, 1864) scales: Chemical characterization and biological activity | |
CN107245094B (zh) | 一种抗氧化肽及其分离制备方法和用途 | |
Islam et al. | Production and antioxidant activity of peptides from sturgeon head | |
CN116284341B (zh) | 一种低免疫原性、降血压、抗氧化的深海鱼皮胶原蛋白肽制备及应用 | |
CN106317170B (zh) | 一种紫苏籽抗氧化肽及其应用 | |
Hazeena et al. | Structural characteristics of collagen from cuttlefish skin waste extracted at optimized conditions | |
Sasidharan et al. | Tuna sidestream valorization: a circular blue bioeconomy approach | |
Chernukha et al. | Comparative study of biocorrective protein-peptide agent to improve quality and safety of livestock products | |
Lu et al. | Identification and characterization of high mobility group box 1 and high mobility group box 2 in Siberian sturgeon (Acipenser baerii) |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
GR01 | Patent grant | ||
GR01 | Patent grant |