Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time
Hypertension, characterized by elevated blood pressure, is commonly treated with angiotensin-I-converting enzyme (ACE) inhibitors. This study evaluated the ACE inhibitory activity (ACEIA) of protein hydrolysate from earthworms (Perionyx excavatus) by commercial proteases. The results showed that the...
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Department of Chemistry, Universitas Gadjah Mada
2025-01-01
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| Series: | Indonesian Journal of Chemistry |
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| Online Access: | https://jurnal.ugm.ac.id/ijc/article/view/99059 |
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| author | Phong Thanh Bui Truc Anh Hoang My Thi Thuy Pham Linh Le Phuong Tran Oanh Kim Nguyen |
| author_facet | Phong Thanh Bui Truc Anh Hoang My Thi Thuy Pham Linh Le Phuong Tran Oanh Kim Nguyen |
| author_sort | Phong Thanh Bui |
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| description | Hypertension, characterized by elevated blood pressure, is commonly treated with angiotensin-I-converting enzyme (ACE) inhibitors. This study evaluated the ACE inhibitory activity (ACEIA) of protein hydrolysate from earthworms (Perionyx excavatus) by commercial proteases. The results showed that the protein hydrolysate of earthworms gave the highest ACEIA of 85.38 ± 2.31% (at the protein concentration of 2 mg/mL) and IC50 value of 844.64 μg/mL when the earthworms were hydrolyzed with Flavourzyme® 500 MG under optimized conditions such as earthworm:phosphate buffer ratio of 1:6 (w/v), hydrolysis temperature of 50 °C, pH 7, enzyme:substrate ratio of 600 U/g protein and hydrolysis time of 2 h. The membrane further fractionated the hydrolysate, and the < 1 kDa fraction had the highest ACEIA with an IC50 value of 261.94 μg/mL. The stability of ACEIA was assessed under various conditions, including in vitro digestion, heat treatment at 100 °C for 180 min, and pH adjustments from pH 1 to 11. The < 1 kDa fraction maintained ACEIA activity at 133.34, 76.25, and 84.95%, respectively, after these treatments. These results suggest that earthworm protein hydrolysates, particularly the <1 kDa fraction, exhibit strong stability and could be promising candidates for the development of functional foods or pharmaceuticals targeting hypertension. |
| format | Article |
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| institution | Kabale University |
| issn | 1411-9420 2460-1578 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Department of Chemistry, Universitas Gadjah Mada |
| record_format | Article |
| series | Indonesian Journal of Chemistry |
| spelling | doaj-art-c05e868786b14cb6a6924d706ec6c4b92025-02-03T04:32:43ZengDepartment of Chemistry, Universitas Gadjah MadaIndonesian Journal of Chemistry1411-94202460-15782025-01-0125113314410.22146/ijc.9905937076Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a TimePhong Thanh Bui0Truc Anh Hoang1My Thi Thuy Pham2Linh Le Phuong Tran3Oanh Kim Nguyen4Department of Food Technology, Faculty of Chemical Engineering, Ho Chi Minh City University of Technology (HCMUT), 268 Ly Thuong Kiet Street, District 10, Ho Chi Minh City 731000, Vietnam; Vietnam National University, Linh Trung Ward, Thu Duc City, Ho Chi Minh City 711000, Vietnam; Hong Bang International University, 215 Dien Bien Phu, Ward 15, Binh Thanh District, Ho Chi Minh City 723000, VietnamHong Bang International University, 215 Dien Bien Phu, Ward 15, Binh Thanh District, Ho Chi Minh City 723000, VietnamHong Bang International University, 215 Dien Bien Phu, Ward 15, Binh Thanh District, Ho Chi Minh City 723000, VietnamHong Bang International University, 215 Dien Bien Phu, Ward 15, Binh Thanh District, Ho Chi Minh City 723000, VietnamHong Bang International University, 215 Dien Bien Phu, Ward 15, Binh Thanh District, Ho Chi Minh City 723000, VietnamHypertension, characterized by elevated blood pressure, is commonly treated with angiotensin-I-converting enzyme (ACE) inhibitors. This study evaluated the ACE inhibitory activity (ACEIA) of protein hydrolysate from earthworms (Perionyx excavatus) by commercial proteases. The results showed that the protein hydrolysate of earthworms gave the highest ACEIA of 85.38 ± 2.31% (at the protein concentration of 2 mg/mL) and IC50 value of 844.64 μg/mL when the earthworms were hydrolyzed with Flavourzyme® 500 MG under optimized conditions such as earthworm:phosphate buffer ratio of 1:6 (w/v), hydrolysis temperature of 50 °C, pH 7, enzyme:substrate ratio of 600 U/g protein and hydrolysis time of 2 h. The membrane further fractionated the hydrolysate, and the < 1 kDa fraction had the highest ACEIA with an IC50 value of 261.94 μg/mL. The stability of ACEIA was assessed under various conditions, including in vitro digestion, heat treatment at 100 °C for 180 min, and pH adjustments from pH 1 to 11. The < 1 kDa fraction maintained ACEIA activity at 133.34, 76.25, and 84.95%, respectively, after these treatments. These results suggest that earthworm protein hydrolysates, particularly the <1 kDa fraction, exhibit strong stability and could be promising candidates for the development of functional foods or pharmaceuticals targeting hypertension.https://jurnal.ugm.ac.id/ijc/article/view/99059aceangiotensin-i-converting enzymehypertensiveperionyx excavatus |
| spellingShingle | Phong Thanh Bui Truc Anh Hoang My Thi Thuy Pham Linh Le Phuong Tran Oanh Kim Nguyen Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time Indonesian Journal of Chemistry ace angiotensin-i-converting enzyme hypertensive perionyx excavatus |
| title | Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time |
| title_full | Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time |
| title_fullStr | Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time |
| title_full_unstemmed | Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time |
| title_short | Optimization of Protein Hydrolysate from Earthworms (<i>Perionyx excavatus</i>) of Angiotensin-I-Converting Enzyme Inhibitory Activity by One Variable at a Time |
| title_sort | optimization of protein hydrolysate from earthworms i perionyx excavatus i of angiotensin i converting enzyme inhibitory activity by one variable at a time |
| topic | ace angiotensin-i-converting enzyme hypertensive perionyx excavatus |
| url | https://jurnal.ugm.ac.id/ijc/article/view/99059 |
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