Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship
Microalgae have gained significant traction as sustainable substitutes for conventional animal-derived proteins, demonstrating remarkable potential as reservoirs of bioactive peptides. This study investigated the application of ultrasonic-assisted enzymatic hydrolysis (UAEH) to extract protein from...
Saved in:
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-06-01
|
| Series: | Future Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666833525000115 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832586179645538304 |
|---|---|
| author | Jeeraporn Pekkoh Apiwit Kamngoen Antira Wichaphian May Thu Zin Supakit Chaipoot Kamon Yakul Wasu Pathom-aree Wageeporn Maneechote Benjamas Cheirsilp Kuan Shiong Khoo Sirasit Srinuanpan |
| author_facet | Jeeraporn Pekkoh Apiwit Kamngoen Antira Wichaphian May Thu Zin Supakit Chaipoot Kamon Yakul Wasu Pathom-aree Wageeporn Maneechote Benjamas Cheirsilp Kuan Shiong Khoo Sirasit Srinuanpan |
| author_sort | Jeeraporn Pekkoh |
| collection | DOAJ |
| description | Microalgae have gained significant traction as sustainable substitutes for conventional animal-derived proteins, demonstrating remarkable potential as reservoirs of bioactive peptides. This study investigated the application of ultrasonic-assisted enzymatic hydrolysis (UAEH) to extract protein from microalgal Chlorella biomass, with the objective of generating peptides possessing angiotensin-converting enzyme (ACE) inhibitory activity. Protein hydrolysates and peptides exhibiting a substantial degree of hydrolysis and bioactivities were achieved following the optimization of ultrasonic-assisted enzymatic hydrolysis (UAEH) under specific conditions: an Alcalase enzyme to microalgal protein loading ratio of 3 %, a hydrolysis temperature of 40 °C, and a hydrolysis duration of 10 min. Interestingly, the fractionated low molecular weight (LMW) peptides (<3 kDa) demonstrated notable levels of both ABTS radical scavenging (IC50 at 3.34 µg/mL) and ACE inhibition activities (IC50 at 2.95 µg/mL), alongside a significant abundance of essential amino acids, reaching up to 34.98 %. Q-TOF-LC-MS/MS analysis of the LMW peptides verified the appearance of active sequences, identifying up to 49 LMW fragments within the fractionated LMW peptides. More importantly, in silico structure-activity relationship analysis proved the non-toxicity of the identified LMW peptides. The result indicates a potential link between 47 LMW peptides and the inhibition of ACE activity, suggesting that microalgae protein hydrolysate and peptides could be developed into new treatments for CVD and hypertension. These findings highlight the promise of microalgae from the UAEH as a source of natural ACE inhibitors or preventative nutritional supplements. |
| format | Article |
| id | doaj-art-2103a1a08d5b4be69ebc3a3a4998683b |
| institution | Kabale University |
| issn | 2666-8335 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Future Foods |
| spelling | doaj-art-2103a1a08d5b4be69ebc3a3a4998683b2025-01-26T05:05:09ZengElsevierFuture Foods2666-83352025-06-0111100548Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationshipJeeraporn Pekkoh0Apiwit Kamngoen1Antira Wichaphian2May Thu Zin3Supakit Chaipoot4Kamon Yakul5Wasu Pathom-aree6Wageeporn Maneechote7Benjamas Cheirsilp8Kuan Shiong Khoo9Sirasit Srinuanpan10Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, ThailandDepartment of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Microbial Biorefinery and Biochemical Process Engineering Research Group, Chiang Mai University, Chiang Mai 50200, ThailandDepartment of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Microbial Biorefinery and Biochemical Process Engineering Research Group, Chiang Mai University, Chiang Mai 50200, ThailandDepartment of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Microbial Biorefinery and Biochemical Process Engineering Research Group, Chiang Mai University, Chiang Mai 50200, ThailandCenter of Excellence in Microbial Diversity and Sustainable Utilization, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Multidisciplinary Research Institute, Chiang Mai University, Chiang Mai 50200, ThailandDivision of Biotechnology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandDepartment of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Center of Excellence in Microbial Diversity and Sustainable Utilization, Faculty of Science, Chiang Mai University, Chiang Mai 50200, ThailandMicrobial Biorefinery and Biochemical Process Engineering Research Group, Chiang Mai University, Chiang Mai 50200, Thailand; Office of Research Administration, Office of the University, Chiang Mai University, Chiang Mai 50200, ThailandProgram of Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, ThailandAlgae Bioseparation Research Laboratory, Department of Chemical Engineering and Materials Science, Yuan Ze University, Taoyuan, TaiwanDepartment of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Microbial Biorefinery and Biochemical Process Engineering Research Group, Chiang Mai University, Chiang Mai 50200, Thailand; Center of Excellence in Microbial Diversity and Sustainable Utilization, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand; Office of Research Administration, Office of the University, Chiang Mai University, Chiang Mai 50200, Thailand; Corresponding author at: Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand.Microalgae have gained significant traction as sustainable substitutes for conventional animal-derived proteins, demonstrating remarkable potential as reservoirs of bioactive peptides. This study investigated the application of ultrasonic-assisted enzymatic hydrolysis (UAEH) to extract protein from microalgal Chlorella biomass, with the objective of generating peptides possessing angiotensin-converting enzyme (ACE) inhibitory activity. Protein hydrolysates and peptides exhibiting a substantial degree of hydrolysis and bioactivities were achieved following the optimization of ultrasonic-assisted enzymatic hydrolysis (UAEH) under specific conditions: an Alcalase enzyme to microalgal protein loading ratio of 3 %, a hydrolysis temperature of 40 °C, and a hydrolysis duration of 10 min. Interestingly, the fractionated low molecular weight (LMW) peptides (<3 kDa) demonstrated notable levels of both ABTS radical scavenging (IC50 at 3.34 µg/mL) and ACE inhibition activities (IC50 at 2.95 µg/mL), alongside a significant abundance of essential amino acids, reaching up to 34.98 %. Q-TOF-LC-MS/MS analysis of the LMW peptides verified the appearance of active sequences, identifying up to 49 LMW fragments within the fractionated LMW peptides. More importantly, in silico structure-activity relationship analysis proved the non-toxicity of the identified LMW peptides. The result indicates a potential link between 47 LMW peptides and the inhibition of ACE activity, suggesting that microalgae protein hydrolysate and peptides could be developed into new treatments for CVD and hypertension. These findings highlight the promise of microalgae from the UAEH as a source of natural ACE inhibitors or preventative nutritional supplements.http://www.sciencedirect.com/science/article/pii/S2666833525000115Angiotensin-I converting enzymeEnzymatic hydrolysisMicroalgaePeptidesProteinUltrasonic |
| spellingShingle | Jeeraporn Pekkoh Apiwit Kamngoen Antira Wichaphian May Thu Zin Supakit Chaipoot Kamon Yakul Wasu Pathom-aree Wageeporn Maneechote Benjamas Cheirsilp Kuan Shiong Khoo Sirasit Srinuanpan Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship Future Foods Angiotensin-I converting enzyme Enzymatic hydrolysis Microalgae Peptides Protein Ultrasonic |
| title | Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship |
| title_full | Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship |
| title_fullStr | Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship |
| title_full_unstemmed | Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship |
| title_short | Production of ACE inhibitory peptides via ultrasonic-assisted enzymatic hydrolysis of microalgal Chlorella protein: Process improvement, fractionation, identification, and in silico structure-activity relationship |
| title_sort | production of ace inhibitory peptides via ultrasonic assisted enzymatic hydrolysis of microalgal chlorella protein process improvement fractionation identification and in silico structure activity relationship |
| topic | Angiotensin-I converting enzyme Enzymatic hydrolysis Microalgae Peptides Protein Ultrasonic |
| url | http://www.sciencedirect.com/science/article/pii/S2666833525000115 |
| work_keys_str_mv | AT jeerapornpekkoh productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT apiwitkamngoen productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT antirawichaphian productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT maythuzin productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT supakitchaipoot productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT kamonyakul productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT wasupathomaree productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT wageepornmaneechote productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT benjamascheirsilp productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT kuanshiongkhoo productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship AT sirasitsrinuanpan productionofaceinhibitorypeptidesviaultrasonicassistedenzymatichydrolysisofmicroalgalchlorellaproteinprocessimprovementfractionationidentificationandinsilicostructureactivityrelationship |