In vitro thrombolytic potential of fibrinolytic enzyme from Brevibacterium sp. isolated from the root of the plant, Aloe castellorum

Abstract

Cardiovascular diseases (CVDs) like stroke and heart attack are leading causes of mortality worldwide, resulting in about 30% of deaths. The proportion in the Kingdom of Saudi Arabia was 46%. The commercial thrombolytic agents are thus associated with a range of side effects, while bacterially derived fibrinolytic enzymes have no or little side effects. Hence, there is an urgent need to identify novel fibrinolytic enzymes to treat or prevent CVDs. An endophytic bacterial strain producing fibrinolytic enzyme was isolated from the root of the plant Aloe castellorum. Enzyme production was enhanced through a conventional method and a statistical approach. The in vitro lytic activity of blood clots was also assessed. Endangered plant of Aloe castellorum roots, researchers isolated an endophytic strain producing fibrinolytic enzymes. It was identified as Brevibacterium sp. The culture medium was also optimized by a conventional method to screen the factors significant for successful culture. Fibrinolytic enzyme production peaked when Brevibacterium sp. was cultured in the presence of maltose (613 ± 12 U/mL), followed by starch (576 ± 13 U/mL). Among the selected nitrogen sources, yeast extract (642 ± 5.9 U/mL) and beef extract (610 ± 13 U/mL) enhanced enzyme yield relative to that in the control (487 ± 7.2 U/mL). Ionic sources such as Mg2+ (672 ± 10.3 U/mL) and Ca2+ (605 ± 12.3 U/mL) showed enhanced fibrinolytic enzyme production relative to the control (405 ± 13.2 U/mL). Upon employing a two-level full factorial design for examining the significant factors, it was revealed that maltose, yeast extract, and Mg2+ were important (p < 0.05). To enhance thrombolytic agent production using central composite design and response surface methodologies. The fibrinolytic enzyme obtained from Brevibacterium sp. has great potential to lyse blood clots in vitro.