Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract
The antimicrobial peptide is a new potential antibiotic type that can be isolated not only from free peptides but also peptides from hydrolyzed protein with proteolytic enzymes. The protein of jatropha seed is toxic due to RIP, ribosome- inactivating protein, and a potential source of AMP. Trifluo...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Rasayan J. Chem.
2022
|
| Subjects: | |
| Online Access: | https://repository.ugm.ac.id/280291/1/Atmawati_PA.pdf |
| _version_ | 1826050418582487040 |
|---|---|
| author | Atmawati, D. R. Andriana, Z. Swasono, Respati Tri Raharjo, Tri Joko |
| author_facet | Atmawati, D. R. Andriana, Z. Swasono, Respati Tri Raharjo, Tri Joko |
| author_sort | Atmawati, D. R. |
| collection | UGM |
| description | The antimicrobial peptide is a new potential antibiotic type that can be isolated not only from free peptides but also
peptides from hydrolyzed protein with proteolytic enzymes. The protein of jatropha seed is toxic due to RIP, ribosome-
inactivating protein, and a potential source of AMP. Trifluoroacetic acid was used to isolate jatropha seed protein. The protein was hydrolyzed using trypsin and the hydrolysate separated with a cation exchange solid phase extraction (SPE) column. Each fraction was tested for antimicrobial activity and resulted in the pH 3 and pH 4 fractions being able to inhibit bacterial growth against Staphylococcus aureus (Gram-positive bacteria) and Escherichia coli (Gramnegative bacteria). The pH 3 fraction has IC50 value 17.95 μg/mL to E. coli and 17.03 μg/mL to S. aureus, while the pH fraction has IC50 value 37.30 μg/mL and 95.31 μg/mL respectively. There are three peptides with amino acid sequences of GAGLVPKR, MGACCSKEPSFAEGR and VALASLLSQPLPQISDK identified from those fractions. These peptides potentially inhibit bacterial growth through membrane destabilization mechanism, due to their amphipathic and ionic properties. |
| first_indexed | 2024-03-14T00:03:40Z |
| format | Article |
| id | oai:generic.eprints.org:280291 |
| institution | Universiti Gadjah Mada |
| language | English |
| last_indexed | 2024-03-14T00:03:40Z |
| publishDate | 2022 |
| publisher | Rasayan J. Chem. |
| record_format | dspace |
| spelling | oai:generic.eprints.org:2802912023-11-09T01:01:59Z https://repository.ugm.ac.id/280291/ Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract Atmawati, D. R. Andriana, Z. Swasono, Respati Tri Raharjo, Tri Joko Chemical Science Mathematics and Applied Sciences The antimicrobial peptide is a new potential antibiotic type that can be isolated not only from free peptides but also peptides from hydrolyzed protein with proteolytic enzymes. The protein of jatropha seed is toxic due to RIP, ribosome- inactivating protein, and a potential source of AMP. Trifluoroacetic acid was used to isolate jatropha seed protein. The protein was hydrolyzed using trypsin and the hydrolysate separated with a cation exchange solid phase extraction (SPE) column. Each fraction was tested for antimicrobial activity and resulted in the pH 3 and pH 4 fractions being able to inhibit bacterial growth against Staphylococcus aureus (Gram-positive bacteria) and Escherichia coli (Gramnegative bacteria). The pH 3 fraction has IC50 value 17.95 μg/mL to E. coli and 17.03 μg/mL to S. aureus, while the pH fraction has IC50 value 37.30 μg/mL and 95.31 μg/mL respectively. There are three peptides with amino acid sequences of GAGLVPKR, MGACCSKEPSFAEGR and VALASLLSQPLPQISDK identified from those fractions. These peptides potentially inhibit bacterial growth through membrane destabilization mechanism, due to their amphipathic and ionic properties. Rasayan J. Chem. 2022 Article PeerReviewed application/pdf en https://repository.ugm.ac.id/280291/1/Atmawati_PA.pdf Atmawati, D. R. and Andriana, Z. and Swasono, Respati Tri and Raharjo, Tri Joko (2022) Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract. Rasayan J. Chem., 15 (2). pp. 1288-1295. ISSN 0976-0083 http://www.rasayanjournal.com http://doi.org/10.31788/RJC.1526892 |
| spellingShingle | Chemical Science Mathematics and Applied Sciences Atmawati, D. R. Andriana, Z. Swasono, Respati Tri Raharjo, Tri Joko Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title | Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title_full | Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title_fullStr | Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title_full_unstemmed | Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title_short | Antibacterial Peptide from Solid Phase Extraction (Spe) Fractionation on Trypsin Hydrolysis of Jatropha (Ricinus communis) Seed Protein Acid Extract |
| title_sort | antibacterial peptide from solid phase extraction spe fractionation on trypsin hydrolysis of jatropha ricinus communis seed protein acid extract |
| topic | Chemical Science Mathematics and Applied Sciences |
| url | https://repository.ugm.ac.id/280291/1/Atmawati_PA.pdf |
| work_keys_str_mv | AT atmawatidr antibacterialpeptidefromsolidphaseextractionspefractionationontrypsinhydrolysisofjatropharicinuscommunisseedproteinacidextract AT andrianaz antibacterialpeptidefromsolidphaseextractionspefractionationontrypsinhydrolysisofjatropharicinuscommunisseedproteinacidextract AT swasonorespatitri antibacterialpeptidefromsolidphaseextractionspefractionationontrypsinhydrolysisofjatropharicinuscommunisseedproteinacidextract AT raharjotrijoko antibacterialpeptidefromsolidphaseextractionspefractionationontrypsinhydrolysisofjatropharicinuscommunisseedproteinacidextract |