Open Access
Thermo-Stable Alkaline Protease Purified from a Novel Endophyte Brevundimonas diminuta VKB1 Hosted in Carica papaya L. – Production Enrichment Approach
Publication year - 2021
Publication title -
biointerface research in applied chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.216
H-Index - 11
ISSN - 2069-5837
DOI - 10.33263/briac116.1437214388
Subject(s) - protease , alkaline protease , carica , biochemistry , chemistry , enzyme , endophyte , chromatography , biology , botany
Protease is the central component of enzymes in all lives, from microbes to humans. Their limited applications in the medicinal field demand their need for higher production. Our study enlightens protease's sustainable production using various optimization techniques and purification of the protease purified from Carica papaya L's endophytes. The results depict that the protease synthesis was enhanced to five-fold concentration after optimization of the production media. The purified protease was a single protein showing high stability towards alkaline pH and thermo-stable. The metal ions' influence indicates that the protease can be catalyzed highly in the presence of copper, magnesium, iron atoms. Results disclose the purified protease further can be taken for pharmacological studies to understand their efficiency as a therapeutic regime.