Unraveling anticancer potential of a novel serine protease inhibitor from marine yeast Candida parapsilosis ABS1 against colorectal and breast cancer cells.
Anticancer activity
Breast cancer
Colorectal cancer
Marine yeast
Protein purification
Serine protease inhibitor
Journal
World journal of microbiology & biotechnology
ISSN: 1573-0972
Titre abrégé: World J Microbiol Biotechnol
Pays: Germany
ID NLM: 9012472
Informations de publication
Date de publication:
10 Jun 2023
10 Jun 2023
Historique:
received:
24
03
2023
accepted:
01
06
2023
medline:
12
6
2023
pubmed:
10
6
2023
entrez:
9
6
2023
Statut:
epublish
Résumé
The study was planned to isolate a serine protease inhibitor compound with anticancer potential against colorectal and breast cancer cells from marine yeast. Protease enzymes play a crucial role in the mechanism of life-threatening diseases like cancer, malaria and AIDS. Hence, blocking these enzymes with potential inhibitors can be an efficient approach in drug therapy for these diseases. A total of 12 marine yeast isolates, recovered from mangrove swamps of Sundarbans, India, showed inhibition activity against trypsin. The yeast isolate ABS1 showed highest inhibition activity (89%). The optimum conditions for protease inhibitor production were found to be glucose, ammonium phosphate, pH 7.0, 30 °C and 2 M NaCl. The PI protein from yeast isolate ABS1 was purified using ethyl acetate extraction and anion exchange chromatography. The purified protein was characterized using denaturing SDS-PAGE, Liquid Chromatography Electrospray Ionization Mass Spectrometry (LC-ESI-MS), Reverse Phase High Pressure Liquid Chromatography (RP-HPLC) and Fourier Transform Infra-red Spectroscopy (FTIR) analysis. The intact molecular weight of the PI protein was determined to be 25.584 kDa. The PI protein was further studied for in vitro anticancer activities. The IC
Identifiants
pubmed: 37296286
doi: 10.1007/s11274-023-03670-9
pii: 10.1007/s11274-023-03670-9
doi:
Substances chimiques
Serine Proteinase Inhibitors
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
225Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature B.V.
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