Purification and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides and the Antihypertensive Effect of Chlorella sorokiniana Protein Hydrolysates

Lin, Yu-Hsin; Chen, Guan-Wen; Yeh, Chin; Song, Helena; Tsai, Jenn-Shou

doi:10.3390/nu10101397

Cited by 57Protein Hydrolysis and Bioactive PeptidesSeaweed-derived Bioactive CompoundsPeptidase Inhibition and Analysis

Purification and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides and the Antihypertensive Effect of Chlorella sorokiniana Protein Hydrolysates

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Lin, Yu-Hsin, Chen, Guan-Wen, Yeh, Chin, Song, Helena, Tsai, Jenn-Shou·2018·Nutrients

DOI 10.3390/nu10101397PMC PMC6213796

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Abstract

Hot water was used to obtain Chlorella sorokiniana hot water extract (HWE). Subsequently, this byproduct was freeze-dried, hydrolysed at 50 °C using Protease N to obtain C. sorokiniana protein hydrolysates (PN-1), and then digested with a gastrointestinal enzyme (PN-1G). The inhibitory effects of the HWE and hydrolysates against angiotensin I-converting enzyme (ACE) were investigated. The soluble protein and peptide contents were 379.9 and 179.7 mg/g, respectively, for HWE and 574.8 and 332.8 mg/g, respectively, for PN-1. The IC50 values of the HWE, PN-1, and PN-1G on ACE were 1.070, 0.035, and 0.044 mg/mL, respectively. PN-1G was separated into seven fractions through size exclusion chromatography. The sixth fraction of the hydrolysate had a molecular weight between 270 and 340 Da, and the lowest IC50 value on ACE was 0.015 mg/mL. The amino acid sequences of the ACE-inhibitory peptides were Trp-Val, Val-Trp, Ile-Trp, and Leu-Trp, of which the IC50 values were 307.61, 0.58, 0.50, and 1.11 µΜ, respectively. Systolic blood pressure and diastolic blood pressure were reduced 20 and 21 mm Hg, respectively, in spontaneously hypertensive rats after 6 h of oral administration with a dose of 171.4 mg PN-1 powder/kg body weight.

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Peptides VECYGPNRPQF from Chlorella vulgaris and tripeptides Trp-Val and Val-Trp from Chlorella sorokiniana exhibit potent ACE inhibition.
“Peptides such as VECYGPNRPQF from Chlorella vulgaris [44] and tripeptides like Trp-Val and Val-Trp from Chlorella sorokiniana [62] exhibit potent ACE inhibition.”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [62]
Section 3.4 identifies Trp–Val and Val–Trp from C. sorokiniana as ACE-inhibitory peptides, supporting the portion attached to citation [62]. They are dipeptides, not tripeptides, and their IC50 values differ markedly: 307.61 μM for Trp–Val versus 0.58 μM for Val–Trp. The claim that both exhibit potent inhibition therefore overstates the result for Trp–Val. (LLM, conf=0.90)
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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Commercial Applications of Microalgae
Spolaore, P., Joannis-Cassan, C., Duran, E., & Isambert, A. (2006) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.101.87 · Cited by 4,285 · see citing works
Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
Cushman, D. W., & Cheung, H. S. (1971) · Biochemical Pharmacology · doi:10.1016/0006-2952(71)90292-9 · Cited by 2,633 · see citing works
Design of Specific Inhibitors of Angiotensin-Converting Enzyme: New Class of Orally Active Antihypertensive Agents
Ondetti, M. A., Rubin, B., & Cushman, D. W. (1977) · Science · doi:10.1126/science.191908 · Cited by 1,866 · see citing works
Spectrophotometric Assay Using o-Phthaldialdehyde for Determination of Proteolysis in Milk and Isolated Milk Proteins
Church, F., Swaisgood, H. E., Porter, D. H., & Catignani, G. L. (1983) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(83)81926-2 · Cited by 1,551 · see citing works
Feasibility of Treating Prehypertension with an Angiotensin-Receptor Blocker
Julius, S., Nesbitt, S. D., Egan, B. M., Weber, M. A., Michelson, E. L., Kaciroti, N., Black, H. R., Grimm, R. H., Messerli, F. H., Oparil, S., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa060838 · Cited by 919 · see citing works
Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.
Cheung, H. S., Wang, F. L., Ondetti, M. A., Sabo, E. F., & Cushman, D. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86187-2 · Cited by 746 · see citing works
Structural Requirements of Angiotensin I-Converting Enzyme Inhibitory Peptides: Quantitative Structure−Activity Relationship Study of Di- and Tripeptides
Wu, J., Aluko, R. E., & Nakai, S. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051263l · Cited by 561 · see citing works
Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
Li, G., Le, G., Shi, Y., & Shrestha, S. (2004) · Nutrition Research · doi:10.1016/j.nutres.2003.10.014 · Cited by 553 · see citing works
Classification and Antihypertensive Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptides Derived from Food Proteins
Iroyukifujita, H., Eiichiyokoyama, K., & Yoshikawa, M. (2000) · Journal of Food Science · doi:10.1111/j.1365-2621.2000.tb16049.x · Cited by 543 · see citing works
Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
Geng, L., Le, G., Shi, Y., et al. (2004) · Nutrition Research · doi:10.1016/s0271-5317(04)00058-2 · Cited by 420 · see citing works
Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides
Wu, J., & Ding, X. (2002) · Food Research International · doi:10.1016/s0963-9969(01)00131-4 · Cited by 344 · see citing works
Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Wakame (Undaria pinnatifida) and Their Antihypertensive Effect in Spontaneously Hypertensive Rats
Sato, M., Hosokawa, T., Yamaguchi, T., Nakano, T., Muramoto, K., Kahara, T., Funayama, K., Kobayashi, A., & Nakano, T. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf020482t · Cited by 290 · see citing works
Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste
Sheih, I.-C., Fang, T. J., & Wu, T.-K. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2008.12.019 · Cited by 280 · see citing works
Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida)
Suetsuna, K., & Nakano, T. (2000) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(00)00110-8 · Cited by 243 · see citing works
Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides from Sake and Sake Lees
Saito, Y., Wanezaki, K., Kawato, A., & Imayasu, S. (1994) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.58.1767 · Cited by 240 · see citing works
Identification of Antihypertensive Peptides from Peptic Digest of Two Microalgae, Chlorella vulgaris and Spirulina platensis
Suetsuna, K., & Chen, J. (2001) · Marine Biotechnology · doi:10.1007/s10126-001-0012-7 · Cited by 219 · see citing works
Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats
Wang, J., Hu, J., Cui, J., Bai, X., Du, Y., Miyaguchi, Y., & Lin, B. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.03.059 · Cited by 212 · see citing works
Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion
Ruiz, J. Á. G., Ramos, M., & Recio, I. (2004) · International Dairy Journal · doi:10.1016/j.idairyj.2004.04.007 · Cited by 193 · see citing works
ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
Tsai, J., Chen, J.-L., & Pan, B. S. (2008) · Process Biochemistry · doi:10.1016/j.procbio.2008.02.019 · Cited by 152 · see citing works
Self-citation
Characterisation of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae
Jang, J., Jeong, S.-C., Kim, J., Lee, Y.-H., Ju, Y., & Lee, J. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.01.010 · Cited by 150 · see citing works
Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk
Tsai, J., Chen, T.-J., Pan, B. S., Gong, S.-D., & Chung, M.-Y. (2007) · Food Chemistry · doi:10.1016/j.foodchem.2007.06.039 · Cited by 120 · see citing works
Self-citation
Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation
Chen, G., Tsai, J., & Pan, B. S. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2006.07.004 · Cited by 120 · see citing works
Self-citation
Antihypertensive Effects, Molecular Docking Study, and Isothermal Titration Calorimetry Assay of Angiotensin I-Converting Enzyme Inhibitory Peptides from Chlorella vulgaris
Xie, J., Chen, X., Wu, J., Zhang, Y., Zhou, Y., Zhang, L., Tang, Y.-J., & Wei, D. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b04294 · Cited by 118 · see citing works
The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme
Tsai, J. S., Lin, T.-P., Chen, J., & Pan, B. S. (2006) · Process Biochemistry · doi:10.1016/j.procbio.2006.05.023 · Cited by 117 · see citing works
Self-citation
Purification and identification of novel angiotensin-I converting enzyme (ACE) inhibitory peptides from cultured marine microalgae (Nannochloropsis oculata) protein hydrolysate
Samarakoon, K. W., O-Nam, K., Ko, J.-Y., Lee, J.-H., Kang, M.-C., Kim, D., Lee, J. B., Lee, J.-S., & Jeon, Y.-J. (2013) · Journal of Applied Phycology · doi:10.1007/s10811-013-9994-6 · Cited by 116 · see citing works
Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate
Wijesekara, I., Qian, Z., Ryu, B., Ngo, D., & Kim, S. (2010) · Food Research International · doi:10.1016/j.foodres.2010.12.022 · Cited by 113 · see citing works
Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein
Pan, S., Wang, S., Jing, L., & Yao, D. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.05.087 · Cited by 110 · see citing works
Isolation of an Antihypertensive Peptide from Alcalase Digest of Spirulina platensis
Lu, J., Ren, D., Xue, Y. Y., Sawano, Y., Miyakawa, T., & Tanokura, M. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf100193f · Cited by 99 · see citing works
Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I‐converting enzyme
Ono, S., Hosokawa, M., Miyashita, K., & Takahashi, K. (2005) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2005.01080.x · Cited by 91 · see citing works
Isolation of Peptides with Angiotensin I‐converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle
Ono, S., Hosokawa, M., Miyashita, K., & Takahashi, K. (2003) · Journal of Food Science · doi:10.1111/j.1365-2621.2003.tb12300.x · Cited by 88 · see citing works
Antihypertensive Effects of Tryptic Hydrolysate of Casein on Normotensive and Hypertensive Volunteers.
Sekiya, S., Kobayashi, Y., Kita, E., Imamura, Y., & Toyama, S. (1992) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.45.513 · Cited by 85 · see citing works
Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis.
Suetsuna, K. (1998) · PubMed · Cited by 78 · see citing works
Modeling the QSAR of ACE-Inhibitory Peptides with ANN and Its Applied Illustration
He, R., Ma, H., Zhao, W., Qu, W., Zhao, J., Luo, L., & Zhu, W. (2011) · International Journal of Peptides · doi:10.1155/2012/620609 · Cited by 70 · see citing works
Novel Angiotensin-Converting Enzyme (ACE) Inhibitory Peptides Derived from Boneless Chicken Leg Meat
Terashima, M., Baba, T., Ikemoto, N., Katayama, M., Morimoto, T., & Matsumura, S. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf100977z · Cited by 64 · see citing works
Measuring Angiotensin-I Converting Enzyme Inhibitory Activity by Micro Plate Assays: Comparison Using Marine Cryptides and Tentative Threshold Determinations with Captopril and Losartan
Henda, Y. B., Labidi, A., Fruitier‐Arnaudin, I., Bridiau, N., Delatouche, R., Maugard, T., Piot, J., Sannier, F., Thiéry, V., & Bordenave-Juchereau, S. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf403004e · Cited by 64 · see citing works
Antihypertensive Effects of Hydrolysates of Wakame (Undaria pinnatifida) and Their Angiotensin-I-Converting Enzyme Inhibitory Activity
Sato, M., Oba, T., Yamaguchi, T., Nakano, T., Kahara, T., Funayama, K., Kobayashi, A., & Nakano, T. (2002) · Annals of Nutrition and Metabolism · doi:10.1159/000066495 · Cited by 63 · see citing works
Novel angiotensin I-converting enzyme inhibitory peptide derived from bovine casein
Yamada, A., Sakurai, T., Ochi, D., Mitsuyama, E., Yamauchi, K., & Abe, F. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.06.089 · Cited by 62 · see citing works
Comparison of different extraction techniques for obtaining extracts from brown seaweeds and their potential effects as angiotensin I-converting enzyme (ACE) inhibitors
Olivares-Molina, A., & Fernández, K. F. (2015) · Journal of Applied Phycology · doi:10.1007/s10811-015-0665-7 · Cited by 59 · see citing works
Synthesis, characterization and antioxidant activity of angiotensin converting enzyme inhibitors
Bhuyan, B. J., & Mugesh, G. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00823k · Cited by 54 · see citing works
Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
Lin, H.-C., Alashi, A., Aluko, R., Pan, B. S., & Chang, Y.-W. (2017) · Food & Nutrition Research · doi:10.1080/16546628.2017.1391666 · Cited by 48 · see citing works
Identification and Quantification of Inhibitors for Angiotensin-Converting Enzyme in Hypoallergenic Infant Milk Formulas
Martin, M., Wellner, A., Ossowski, I., & Henle, T. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf800865b · Cited by 44 · see citing works
Angiotensin I-Converting Enzyme Inhibitory Action of Fish Sauce.
(KAINUMA), A. O., Matsumoto, E., IWASHITA, A., Yasuhara, T., Kawamura, Y., KOIZUMI, Y., & YANAGIDA, F. (1995) · Food Science and Technology International Tokyo · doi:10.3136/fsti9596t9798.1.101 · Cited by 40 · see citing works
Separation and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Peptic Digest of Hizikia fusiformis Protein.
Suetsuna, K. (1998) · NIPPON SUISAN GAKKAISHI · doi:10.2331/suisan.64.862 · Cited by 39 · see citing works
Purification and identification of an angiotensin I-converting enzyme inhibitory peptide from cauliflower by-products protein hydrolysate
Xu, Y., Bao, T., Han, W., Chen, W., Zheng, X., & Wang, J. (2016) · Process Biochemistry · doi:10.1016/j.procbio.2016.05.023 · Cited by 33 · see citing works
Antioxidant activity of peptide-based angiotensin converting enzyme inhibitors
Bhuyan, B. J., & Mugesh, G. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob06533a · Cited by 30 · see citing works
Acute Tubular Necrosis due to Captopril
Shohaib, S. A., & Raweily, E. A. (2000) · American Journal of Nephrology · doi:10.1159/000013573 · Cited by 20 · see citing works
Effect of Chlorella on blood pressure, cerebral stroke lesions, hypertensive vascular changes and life-span in spontaneously hypertensive rats.
Murakami, T., Okamoto, K., Ogaki, M., & Iizuka, Y. (1987) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.40.351 · Cited by 20 · see citing works
CARDIOVASCULAR EFFECTS OF WHEY FROM PROZYME 6-FACILITATED LACTIC ACID BACTERIA FERMENTATION OF MILK
Chen, G., Tsai, J., & Pan, B. S. (2007) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.2007.00135.x · Cited by 10 · see citing works
Self-citation
Synthesis of 1-((S)-3-acetylthio-2-methylpropanoyl)-L-propyl-L-phenylalanine (alacepril) and one of its active metabolites, the desacetyl derivative (DU-1227).
SAWAYAMA, T., Itokawa, A., Shimada, K., Yasumasa, D. O. I., KIMURA, Y., & Nishimura, H. (1990) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.38.529 · Cited by 7 · see citing works

Flagged first, then by citations

Research works printed but not linked: 4

[33]Cooper T.G. Spectrophotometry The Tools of Biochemistry 1st ed. Wiley-Interscience Hoboken, NJ, USA 1977 53 55 0471171166
[39]SAS Institute Inc. SAS/STAT User’s Guide SAS Institute Press Cary, NC, USA 1988 584
[54]Cheung H.S. Wang F.L. Ondetti M.A. Sabo E.F. Cushman D.W. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme J. Biol. Chem. 1980 255 401 407 6243277
[55]Xiao G. Yanhan H. Jing L. Jing L. Zhu S. Fei H. Binding modes between C-domain selective angiotensin-converting enzyme (ACE) inhibitory dipeptides and ACE domains Food Sci. 2017 38 160 166 10.7506/spkx1002-6630-201705026 · DOI

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de Amorim, A. P., SILVA, G. H. D., Costa, R. M. P. B., Porto, A. L. F., & Bezerra, R. P. (2022) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765202220201636 · Cited by 18 · see citing works
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Suo, Q., Wang, J., Wu, N., Geng, L., Zhang, Q., & Yang, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135873 · Cited by 18 · see citing works
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Kurniawan, R., Taslim, N. A., Hardinsyah, H., Syauki, A. Y., Idris, I., Aman, A. M., Permatasari, H. K., Wiyarta, E., Surya, R., Mayulu, N., et al. (2024) · Future Foods · doi:10.1016/j.fufo.2024.100354 · Cited by 14 · see citing works
Production, characterization and bio-functional properties of multi-functional peptides from fermented plant-based foods: A review
Bhuva, B., Gawai, K. M., Singh, B. P., Sarkar, P., Hassan, M. Z., Kovaleva, E. G., & Hati, S. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.105877 · Cited by 14 · see citing works
Food-derived Trp-rich oligopeptides: Production, bioactivities, and structure-function relationship
Wu, J., Cui, C., & Sun‐Waterhouse, D. (2023) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2023.104247 · Cited by 13 · see citing works
Recent advances of silk‐fibroin‐based hydrogel in the field of antibacterial application
Zou, P., Li, X., Zhao, H., Qu, S., Jiang, Z., Xi, L., Wu, C., & Liu, L. (2024) · Polymer International · doi:10.1002/pi.6699 · Cited by 13 · see citing works
Bioactive Peptides from Microalgae and Cyanobacteria and Their Possible Mechanisms of Action
Chitthan, S. V., Rasheed, A. S., Muniyandi, M., Dhanasekaran, D., & Thajuddin, N. (2025) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-025-10746-7 · Cited by 12 · see citing works
Carbohidratos y proteínas en microalgas: potenciales alimentos funcionales
Galarza, V. O. (2019) · Brazilian journal of food technology/Brazilian Journal of Food Technology · doi:10.1590/1981-6723.04319 · Cited by 10 · see citing works
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Ferdous, U. T., Khan, S. A., Shakoor, A., Uddin, S., Nazarudin, M. F., & Zia, A. W. (2025) · Food Reviews International · doi:10.1080/87559129.2025.2493740 · Cited by 8 · see citing works
Microalgae-Derived Peptides Targeting Lifestyle-Related Diseases: Discovery, Mechanisms, Structure–Activity Relationships, and Structural Modifications
Qoms, M. S., Wong, S. K., Fauzi, N. M., Husain, K., Makpol, S., & Tan, J. K. (2025) · Antioxidants · doi:10.3390/antiox14101170 · Cited by 8 · see citing works
Identification of Novel Nonapeptides from Sipunculus nudus L. and Comparing Its ACEI Activities Mechanism by Molecular Docking
Qi, Y., Tang, X., Liu, H., Lin, Q., Lu, Y., & Luo, H. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10328-3 · Cited by 8 · see citing works
Chlorella sp. as a promising protein source: insight to novel extraction techniques, nutritional and techno-functional attributes of derived proteins
Bakshi, S., Kanetkar, P., Bunkar, D. S., Browne, C., & Paswan, V. K. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2491646 · Cited by 7 · see citing works
Discovery and molecular mechanism of a novel antihypertensive peptide from Chlamydomonas reinhardtii based on molecular docking, molecular dynamics simulation, in vitro, and in vivo analysis
Suo, Q., Yue, Y., Wang, J., Wu, N., Geng, L., & Zhang, Q. (2026) · Food Research International · doi:10.1016/j.foodres.2026.118477 · Cited by 6 · see citing works
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Ganesan, A. R., Munisamy, S., Bhat, R., Seedevi, P., Mohan, K., & Matsukawa, S. (2021) · Wiley eBooks · doi:10.1002/9781119542650.ch14 · Cited by 5 · see citing works
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Khaliq, M., Noor, Z., Moazzam, M., Saeed, F., Tul-Zohra, K., Tariq, E., Muhammad Shahbaz, H., & Khaliq, K. (2026) · Annals of Medicine · doi:10.1080/07853890.2026.2637282 · Cited by 4 · see citing works
“Trp-Val and Val-Trp from Chlorella sorokiniana [62] exhibit potent ACE inhibition.”
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Culețu, A., Kreische, M., Schweikert, T., Henze, A., & Sagu, S. T. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148081 · Cited by 3 · see citing works
Recent advances in the production and use of the edible microalga Chlorella sorokiniana
Salinas-García, M., Villaró‐Cos, S., Cáceres-Ferroni, F., & Lafarga, T. (2026) · Journal of Applied Phycology · doi:10.1007/s10811-026-03931-8 · Cited by 3 · see citing works
Antihyperglycemic activity of colostrum peptides
Тихонов, С. Л., Тихонова, Н. В., Гетте, И. Ф., Sokolova, K. V., & Danilova, I. G. (2023) · Foods and raw materials · doi:10.21603/2308-4057-2024-1-586 · Cited by 3 · see citing works
Biological activity and health benefits of food-derived bioactive peptides
Panbangred, W. (2022) · ScienceAsia · doi:10.2306/scienceasia1513-1874.2022.107 · Cited by 1 · see citing works
Algal peptides for future food: Key players and multifaceted agents in the fight against cardiometabolic syndrome
Baravia, P. A., Qhabibi, F. R., Hadinata, E., Katuuk, S. H. H., Alfaray, R. I., Rampengan, D. D. C. H., Syahputra, R. A., Taslim, N. A., Tjandrawinata, R. R., Tallei, T. E., et al. (2025) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2025.101786 · Cited by 1 · see citing works
Protease inhibitory activity profile of Indonesia wild swamp eel (Monopterus albus)
Nopianti, R., Chasanah, E., Sukarno, S., & Suhartono, M. T. (2023) · Food Research · doi:10.26656/fr.2017.7(1).707 · Cited by 1 · see citing works
The Effect of the Aqueous Suspension of Chlorella Vulgaris on Functional Systems in Healthy People
PLAKIDA, A. L., Yushkovskaya, O. G., Filonenko, A., & Gushcha, S. (2020) · Acta Balneologica · doi:10.36740/abal202001103
ANÁLISE DAS INTOXICAÇÕES EXÓGENAS REGISTRADAS PELO SISTEMA DE INFORMAÇÃO DE AGRAVOS DE NOTIFICAÇÃO NO DISTRITO FEDERAL NO PERÍODO DE 2015 A 2019
da Cunha, B. L. D. S., Silveira, G. A. F., & Ribeiro, I. F. (2021) · Amplla Editora eBooks · doi:10.51859/amplla.csa528.2121-19
OS EFEITOS DO CUIDADO MÃE CANGURU EM RECÉM-NASCIDOS PREMATUROS: UMA REVISÃO INTEGRATIVA
Marques, G. S., Carvalho, A. D., & Veiga, I. N. (2021) · Amplla Editora eBooks · doi:10.51859/amplla.csa528.2121-5
Avaliação dos efeitos da proteína de frango hidrolisada por processo enzimático na pressão arterial e microbiota retal de felinos idosos e obesos: um modelo para hipertensão humana
Príncipe, L. D. A. (2024) · doi:10.11606/d.10.2024.tde-16052024-134808
Functional proteins and peptides from microalgae
Silva, S. C., Colla, E., Dias, M. M., & Barreiro, M. F. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-22080-7.00023-5
Preventive effects of microalgae-based supplements on risk factors associated with metabolic syndrome
Vieira, M. V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-22080-7.00037-5
Assessment of Marine Microalgae's Bioactive Extracts Potential for Food Applications
Sousa, V. E. D. S., Coelho, M., Martins, J., Pereira, R. N., Maciel, F., Pintado, M. E., Dias, Ó., Vicente, A. A., & Geada, P. (2026) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.70398
Edible proteins and bioactive peptides from microalgae
García-Maldonado, E. D., García-Rodríguez, P. G., Barriga, C. M.-D., Sandoval-Sánchez, M. F., Jacuinde-Ruíz, J. C., & González‐Hernández, J. C. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34082-6.00022-2
Novel and ancestral α-amino acid ester acyltransferases with higher thermostability for dipeptide synthesis
Amoroso, C., Puc, J., Maresch, D., Tran, A.-M., & Peterbauer, C. (2026) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2026.110917
Pariset: A primary dataset for therapeutic algal peptides focusing on antihypertensive, antioxidative, antibacterial, antihyperglycemic, and anticancer activities
Karimi, I., Olfati, P., Yousofvand, N., Mohammed, L. J., & Schiöth, H. B. (2026) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2026.100728

A novel angiotensin I-converting enzyme (ACE) inhibitory peptide from a marine Chlorella ellipsoidea and its antihypertensive effect in spontaneously hypertensive rats
Ko, S., Kang, N., Kim, E.-A., Kang, M. C., Lee, S., Kang, S., Lee, J.-B., Jeon, B.-T., Kim, S., Park, S., et al. (2012) · Process Biochemistry · doi:10.1016/j.procbio.2012.07.015 · Cited by 193 · see citing works
Purification of a Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptide with an Antihypertensive Effect from Loach (Misgurnus anguillicaudatus)
Li, Y., Zhou, J., Huang, K., Sun, Y., & Zeng, X. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf204118n · Cited by 61 · see citing works
Identification of an Angiotensin I‐converting Enzyme Inhibitory Peptides from Protein Hydrolysates by a Soybean Protease and the Antihypertensive Effects of Hydrolysates in 4 Spontaneously Hypertensive Model Rats
Kodera, T., & Nio, N. (2006) · Journal of Food Science · doi:10.1111/j.1365-2621.2006.tb15612.x · Cited by 111 · see citing works
A novel angiotensin I-converting enzyme inhibitory peptide from Phascolosoma esculenta water-soluble protein hydrolysate
Du, L., Fang, M., Wu, H., Xie, J., Wu, Y., Li, P., Zhang, D., Huang, Z., Xia, Y., Zhou, L., et al. (2013) · Journal of Functional Foods · doi:10.1016/j.jff.2012.12.003 · Cited by 49 · see citing works
Antihypertensive Action of the Orally Administered Protease Hydrolysates of Chum Salmon Head and Their Angiotensin I-Converting Enzyme Inhibitory Peptides.
Ohta, T., IWASHITA, A., Sasaki, S., & Kawamura, Y. (1997) · Food Science and Technology International Tokyo · doi:10.3136/fsti9596t9798.3.339 · Cited by 22 · see citing works

Authors: Lin, Y.-H., Chen, G.-W., Yeh, C., Song, H., & Tsai, J.-S.
Affiliations: Department of Food Technology and Marketing, Taipei University of Marine Technology, No. 212, Section 9, Yan Ping North Road, Taipei 111, Taiwan
Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung 202, Taiwan
Taiwan Chlorella Manufacturing Co., Ltd., 5 F, No. 71, Section 2, Nan-King East Road, Taipei 104, Taiwan
National Taiwan Ocean University (TW)
ORCID: Lin, Yu-Hsin
Venue: Nutrients
Publisher: MDPI AG
Published: 2018-10-01
Volume: 10
Issue: 10
Pages: 1397
ISSN: 2072-6643 (ISSN-L)
DOI: 10.3390/nu10101397
PMC: PMC6213796
OpenAlex: W2894206255
Cited by: 57
References: 49
Citations by year: 2026: 8 · 2025: 12 · 2024: 8 · 2023: 4 · 2022: 5 · 2021: 11 · 2020: 4 · 2019: 5
FWCI: 1.78
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Nutrients (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, other-oa)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Science Council (NSC98-2321-B-019-002)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
Keywords: ACE inhibitors, bioactive peptides, Chlorella sorokiniana, protein hydrolysates, antihypertensive effect, peptide purification, amino acid sequence, gastrointestinal digestion, spontaneously hypertensive rats, blood pressure reduction
MeSH terms: Amino Acid Sequence, Angiotensin-Converting Enzyme Inhibitors, Animals, Antihypertensive Agents, Blood Pressure, Chlorella, Chromatography, Gel, Hypertension, Male, Molecular Weight, Peptides, Protein Hydrolysates, Rats, Inbred SHR, Rats

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Purification and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides and the Antihypertensive Effect of Chlorella sorokiniana Protein Hydrolysates

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