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Journal : INDONESIAN JOURNAL OF MEDICAL LABORATORY SCIENCE AND TECHNOLOGY

In vitro anticoagulant activity of crude fibrinolytic protease HSFT-2 as an alternative anticoagulant agent Afriansyah, Muhammad Ardi; Rahajoe, Toeti; Pranindira, Raksi
JURNAL INDONESIA DARI ILMU LABORATORIUM MEDIS DAN TEKNOLOGI Vol 7 No 1 (2025): Advances in biomarkers, therapeutics, and probiotics: Recent updates in medical l
Publisher : Universitas Nahdlatul Ulama Surabaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33086/ijmlst.v7i1.5758

Abstract

Thrombotic disorders are one of the leading causes of death in cardiovascular patients and contribute to the incidence of non-infectious diseases. The search for new anticoagulant agents to overcome the limitations associated with existing anticoagulant therapies is increasing, especially those derived from natural and microbial sources. Staphylococcus hominis HSFT-2 is a Gram-positive coccus isolated from rusip Holothutia scabra commonly known as sand sea cucumber. Fibrinolytic protease HSFT-2 has been reported to be able to degrading fibrin, which has shown several characteristics of fibrinolytic and clot-lysis activities. This study aims to evaluate the anticoagulant activity of crude fibrinolytic protease HSFT-2 in vitro as potential alternative anticoagulant agents. The research design was completely randomized, with a sample size of 21 participants calculated using the Federer formula. The material used was crude protease derived from S. hominis cultured in Skim Milk Broth. Various tests, including blood routine tests, platelet aggregation tests, and blood smear evaluations, were conducted to assess its effectiveness as an anticoagulant. Whole blood samples were divided into three groups: a positive control, a negative control, and a group treated directly with 100 µL of crude fibrinolytic protease. The normality of the data was evaluated using the Kruskal-Wallis test, while differences between groups were analyzed with one-way ANOVA. The one-way ANOVA results from the blood routine tests indicated a significant difference between the control and the fibrinolytic protease HSFT-2 (p<0.05). The platelet aggregation percentage decreased from 75.85% in the control group to 21.75% with the addition of crude protease HSFT-2. Furthermore, the blood smear evaluations revealed no abnormalities in cell formation when HSFT-2 protease was used, compared to samples without the addition of EDTA anticoagulant. In conclusion, the fibrinolytic protease HSFT-2 exhibits anticoagulant activity; however, it does not yet meet the standards required for use as an anticoagulant in routine blood tests. Future work should focus on the purification and characterization of the protease to enhance its anticoagulant potential for laboratory diagnostic applications.
Exploration and molecular identification of proteolytic bacteria from rusip pacific oyster (Crassostrea gigas) as anticoagulant agent candidates Afriansyah, Muhammad Ardi; Sudarwin; Dewi, Sri Sinto; Akbar, Gusti Dimas Refian
JURNAL INDONESIA DARI ILMU LABORATORIUM MEDIS DAN TEKNOLOGI Vol 7 No 1 (2025): Advances in biomarkers, therapeutics, and probiotics: Recent updates in medical l
Publisher : Universitas Nahdlatul Ulama Surabaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33086/ijmlst.v7i1.6083

Abstract

The marine symbiont Staphylococcus epidermidis strain CGF-6, a protease-producing bacterium, has been successfully isolated from Rusip Pacific Oyster (Crassostrea gigas). S. epidermidis is a non-spore-forming, Gram-positive coccus commonly found in marine environments due to their ability to tolerate high salinity. The aim of this study was to identify proteolytic bacteria from Rusip fermented C. gigas as potential candidates for the development of anticoagulant agents. Bacterial isolation was performed through the fermentation process of Rusip. After seven days, bacterial colonies were purified three times using Nutrient Agar. The selection of proteolytic bacterial was conducted qualitatively using a skim milk agar medium. The bacterial isolates exhibiting the highest protease activity were identified through 16S rRNA gene sequencing using universal primers Bact 27F and UniB 1492R. Phylogenetic tree analysis, conducted with the MEGA X program, helped determine the relationships between species. Out of the 18 bacterial isolates obtained from the Rusip fermentation of C. gigas, three isolates (CGF-1, CGF-6, and CGF-11) exhibited hydrolysis zones around their colonies on skim milk agar, indicating protease activity.  Among these, isolate CGF-6 showed the highest proteolytic index of 0.5 and was identified as Staphylococcus epidermidis strain CGF-6. S. epidermidis strain CGF-6 has the potential to serve as a valuable source of protease production for the development of anticoagulant agents. However, further studies, including enzyme characterisation, optimisation, and both in vitro and in vivo anticoagulant activity tests, are necessary to assess the efficacy and safety of this enzyme as a candidate for anticoagulant agents.