Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis
Gracilaria lemaneiformis were prepared by enzymatic hydrolysis with molecular weight <1 kDa,collecting peptide components by freeze drying and spray drying,measuring the activity retention rate and antioxidant capacity of ACE inhibitory peptides in the in vitro environment. The antioxidant capaci...
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The editorial department of Science and Technology of Food Industry
2022-04-01
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Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080345 |
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author | Jiasen SHEN Yongchang SU Xiaoting CHEN Shuji LIU Min XU Zhiyu LIU Hetong LIN |
author_facet | Jiasen SHEN Yongchang SU Xiaoting CHEN Shuji LIU Min XU Zhiyu LIU Hetong LIN |
author_sort | Jiasen SHEN |
collection | DOAJ |
description | Gracilaria lemaneiformis were prepared by enzymatic hydrolysis with molecular weight <1 kDa,collecting peptide components by freeze drying and spray drying,measuring the activity retention rate and antioxidant capacity of ACE inhibitory peptides in the in vitro environment. The antioxidant capacity and in vitro stability of peptides were determined by experiments of inhibition of angiotensin converting enzyme activity, total antioxidant capacity, DPPH· scavenging capacity, hydroxyl free radical scavenging capacity and superoxide anion scavenging capacity. The results showed that by using ACE inhibitory activity as indicators, both had good IC50 values (0.62, 0.70 mg/mL) in ACE inhibitory activity. The addition of metal ions (Zn2+、Cu2+) were both promoted inhibitory activity retention,(Al3+、K+、Fe3+) were retained the ACE inhibitory activity of GLP-F and GLP-S, Ca2+reduced the ACE inhibitory activity of both. With the increase of NaCl concentration, the ACE inhibitory activity was reduced of GLP-F and GLP-S; under high sugar concentration, GLP-F was better retained, and GLP-S activity was significantly increased(P<0.05). With strong acid and alkali, GLP-F activity retention decreased by 5%, GLP-S inhibitory activity remained unchanged with pH 4~10. Below 40 ℃, the ACE inhibitory activity was stabled of GLP-F and GLP-S. Simulation the digestion of gastrointestinal tract, GLP-F belonged to pro-drug type, GLP-S belonged to true inhibitor type. GLP-F and GLP-S suited for storage at −20 °C, GLP-F activity retention decreased to 40.67% stored at 4 ℃ until 14 d. The results of above antioxidant tests indicated that GLP-S had superior in terms of total antioxidant activities, DPPH· free radicals, ·OH and O2−· than GLP-F. Therefore, the stability of GLP-F polypeptide in lowering blood pressure activity in vitro had better than that of GLP-S, and GLP-S had more effective than GLP-F in anti-oxidation. Gracilaria lemaneiformis polypeptide providing theoretical reference for the development of natural antihypertensive peptides and antioxidant peptides. |
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spelling | doaj.art-f32efd8c67f04fe9a2447956da2a6b2c2022-12-22T03:39:33ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062022-04-0143738439210.13386/j.issn1002-0306.20210803452021080345-7Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformisJiasen SHEN0Yongchang SU1Xiaoting CHEN2Shuji LIU3Min XU4Zhiyu LIU5Hetong LIN6Engineering Research Centre of Fujian-Taiwan Special Marine Food Processing and Nutrition, Ministry of Education, Fuzhou 350002, ChinaFisheries Research Institute of Fujian, National Research and Development Center for Marine Fish Processing, Key Laboratory of Cultivation and High-value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, ChinaFisheries Research Institute of Fujian, National Research and Development Center for Marine Fish Processing, Key Laboratory of Cultivation and High-value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, ChinaFisheries Research Institute of Fujian, National Research and Development Center for Marine Fish Processing, Key Laboratory of Cultivation and High-value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, ChinaFisheries Research Institute of Fujian, National Research and Development Center for Marine Fish Processing, Key Laboratory of Cultivation and High-value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, ChinaFisheries Research Institute of Fujian, National Research and Development Center for Marine Fish Processing, Key Laboratory of Cultivation and High-value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, ChinaEngineering Research Centre of Fujian-Taiwan Special Marine Food Processing and Nutrition, Ministry of Education, Fuzhou 350002, ChinaGracilaria lemaneiformis were prepared by enzymatic hydrolysis with molecular weight <1 kDa,collecting peptide components by freeze drying and spray drying,measuring the activity retention rate and antioxidant capacity of ACE inhibitory peptides in the in vitro environment. The antioxidant capacity and in vitro stability of peptides were determined by experiments of inhibition of angiotensin converting enzyme activity, total antioxidant capacity, DPPH· scavenging capacity, hydroxyl free radical scavenging capacity and superoxide anion scavenging capacity. The results showed that by using ACE inhibitory activity as indicators, both had good IC50 values (0.62, 0.70 mg/mL) in ACE inhibitory activity. The addition of metal ions (Zn2+、Cu2+) were both promoted inhibitory activity retention,(Al3+、K+、Fe3+) were retained the ACE inhibitory activity of GLP-F and GLP-S, Ca2+reduced the ACE inhibitory activity of both. With the increase of NaCl concentration, the ACE inhibitory activity was reduced of GLP-F and GLP-S; under high sugar concentration, GLP-F was better retained, and GLP-S activity was significantly increased(P<0.05). With strong acid and alkali, GLP-F activity retention decreased by 5%, GLP-S inhibitory activity remained unchanged with pH 4~10. Below 40 ℃, the ACE inhibitory activity was stabled of GLP-F and GLP-S. Simulation the digestion of gastrointestinal tract, GLP-F belonged to pro-drug type, GLP-S belonged to true inhibitor type. GLP-F and GLP-S suited for storage at −20 °C, GLP-F activity retention decreased to 40.67% stored at 4 ℃ until 14 d. The results of above antioxidant tests indicated that GLP-S had superior in terms of total antioxidant activities, DPPH· free radicals, ·OH and O2−· than GLP-F. Therefore, the stability of GLP-F polypeptide in lowering blood pressure activity in vitro had better than that of GLP-S, and GLP-S had more effective than GLP-F in anti-oxidation. Gracilaria lemaneiformis polypeptide providing theoretical reference for the development of natural antihypertensive peptides and antioxidant peptides.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080345ace inhibitory peptidesstabilityantioxidantstoragegracilaria lemaneiformis proteinanti-hypertension |
spellingShingle | Jiasen SHEN Yongchang SU Xiaoting CHEN Shuji LIU Min XU Zhiyu LIU Hetong LIN Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis Shipin gongye ke-ji ace inhibitory peptides stability antioxidant storage gracilaria lemaneiformis protein anti-hypertension |
title | Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis |
title_full | Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis |
title_fullStr | Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis |
title_full_unstemmed | Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis |
title_short | Study on in Vitro Stability and Antioxidant Activity of ACE Inhibitory Peptide from Gracilaria lemaneiformis |
title_sort | study on in vitro stability and antioxidant activity of ace inhibitory peptide from gracilaria lemaneiformis |
topic | ace inhibitory peptides stability antioxidant storage gracilaria lemaneiformis protein anti-hypertension |
url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080345 |
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