Fibrinolytic bacteria of Indonesian fermented soybean: preliminary study on enzyme activity and protein profile

Syahbanu, Fathma; Kezia, Elisabeth; Puera, Narwastu; Giriwono, Puspo Edi; Tjandrawinata, Raymond Ruby; Suhartono, Maggy Thenawidjaja

doi:10.1590/fst.23919

Cited by 11 publications

(5 citation statements)

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“…Our earlier work has shown that the Subtilisin K2 enzyme of Indonesian moromi is capable of hydrolyzing fibrin, as shown Molecular docking of Subtilisin K2, a fibrin-degrading enzyme from Indonesian moromi, with its substrates by the fibrin plate assay (Syahbanu et al, 2020a), as well as hydrolyzing fibrinogen in fibrinogen zymogram analysis (Syahbanu et al, 2020b). The present bioinformatic work was carried out to elucidate in more detail the mode of this interaction with the substrates fibrin and fibrinogen.…”

Section: Introductionmentioning

confidence: 83%

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Molecular docking of Subtilisin K2, a fibrin-degrading enzyme from Indonesian moromi, with its substrates

et al. 2022

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Fibrinogen supplies the primary building block of the blood clot or thrombus after α-thrombin converts fibrinogen to fibrin during the final phases of coagulation. When the homeostasis system is disrupted, blood clots that aggregate in the blood vessels can lead to thrombosis. Fibrin-degrading enzyme from Bacillus subtilis K2 (Subtilisin K2) of Indonesian moromi has many excellent characteristics apart from its strong fibrinolytic activity. Bioinformatic analysis using the CDART webserver indicated that the enzyme appeared to share a conserved domain with the peptidase s8 superfamily also known as the subtilase family. This study used molecular docking between these fibrin-degrading enzymes and specific substrates (fibrin and fibrinogen) using the HADDOCK webserver and aimed to predict the enzyme mechanism of action. This analysis revealed that the enzyme interlocked with the two substrates; however, it suggested no productive interactions between Subtilisin K2 and fibrinogen. A hydrolysis reaction is suggested between Subtilisin K2 and the fibrin substrate. There was a strong indication that amino acids Asp19, His51, and Ser208 in Subtilisin K2's active site interacts with Leu168, Ile171, and Leu172 of the fibrin substrate with a ∆G of -19.4 kcal/mol. Subtilisin K2 tends to act more as a fibrin-degrading enzyme than as a fibrinogen-degrading enzyme.

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Section: Introductionmentioning

confidence: 83%

“…The protein sequence of the fibrin-degrading enzyme Subtilisin K2 from Bacillus subtilis K2 (this isolate originated from moromi and was previously collected (Syahbanu et al, 2020a)) was retrieved from GenBank (accession number: MN294987). Subtilisin K2 consists of 262 amino acids, and the sequence data were saved in the FASTA format.…”

Section: Methodsmentioning

confidence: 99%

Molecular docking of Subtilisin K2, a fibrin-degrading enzyme from Indonesian moromi, with its substrates

et al. 2022

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“…Fermented soybeans have been consumed as traditional foods in many Asian countries, and indeed, they are sources of nattokinase and other fibrinolytic enzymes. These includes natto, a Japanese traditional fermented soybean obtained from fermentation with Bacillus subtilis G8 and Bacillus subtilis (Chang et al, 2012;Lucy et al, 2019), moromi, oncom and gambus (Indonesian traditional fermented soybean obtained from fermentation with Bacillus cereus, Bacillus subtilus, Bacillus pumilus, and Stenotrophomonas sp, respectively) (Afifah et al, 2014;Nailufar et al, 2016;Stephani et al, 2017;Syahbanu et al, 2020) as well as douchi and doufuru (Chinese traditional fermented soybean obtained from fermentation with Bacillus (Ok and Choi, 2005;Wang et al, 2006;Jo et al, 2011;Wei et al, 2011;Yuan et al, 2012;Chen et al, 2013;Heo et al, 2013;Park et al, 2013;Gad et al, 2014;Thokchom and Joshi, 2014;Bi et al, 2015;Huy et al, 2016;Liu et al, 2016;Nailufar et al, 2016;Hu et al, 2019;Ito, 2020;Syahbanu et al, 2020 (Shirasaka et al, 2012;Biji et al, 2016;Vijayaraghavan et al, 2016a;Vijayaraghavan et al, 2016b;Vijayaraghavan et al, 2019), seafood fermented with Bacillus sp, Bacillus. velezensis BS2, Bacillus pumilus BS15 and Bacillus coagulans (Anh et al, 2015;Prihanto and Firdaus, 2019;Yao et al, 2019;Kim et al, 2020) and liquors obtained from fermentation with Bacillus amyloliquefaciens, Bacillus licheniformis and Bacillus-Genus (Lapsongphon et al, 2013;Johnson e...…”

Section: Microorganisms As Sources Of Fibrinolytic Enzymesmentioning

confidence: 99%

Role of Fibrinolytic Enzymes in Anti-Thrombosis Therapy

Altaf

Kasim

2021

Front. Mol. Biosci.

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Thrombosis, a major cause of deaths in this modern era responsible for 31% of all global deaths reported by WHO in 2017, is due to the aggregation of fibrin in blood vessels which leads to myocardial infarction or other cardiovascular diseases (CVDs). Classical agents such as anti-platelet, anti-coagulant drugs or other enzymes used for thrombosis treatment at present could leads to unwanted side effects including bleeding complication, hemorrhage and allergy. Furthermore, their high cost is a burden for patients, especially for those from low and middle-income countries. Hence, there is an urgent need to develop novel and low-cost drugs for thrombosis treatment. Fibrinolytic enzymes, including plasmin like proteins such as proteases, nattokinase, and lumbrokinase, as well as plasminogen activators such as urokinase plasminogen activator, and tissue-type plasminogen activator, could eliminate thrombi with high efficacy rate and do not have significant drawbacks by directly degrading the fibrin. Furthermore, they could be produced with high-yield and in a cost-effective manner from microorganisms as well as other sources. Hence, they have been considered as potential compounds for thrombosis therapy. Herein, we will discuss about natural mechanism of fibrinolysis and thrombus formation, the production of fibrinolytic enzymes from different sources and their application as drugs for thrombosis therapy.

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“…Recently, the starter cultures have been applied into fermented foods to improve their nutritional quality and prolong shelf life. These starter cultures could induce the production of bacteriocin or acidic byproducts, which could inhibit the growth of foodborne pathogens (Kim et al, 2018;Syahbanu et al, 2020). It is noteworthy that L. sakei can thrive in high-salt, low-water, low-temperature, and low pH conditions (Chiaramonte et al, 2009), and has an ability to produce bacteriocins to inhibit pathogenic bacteria (Aasen et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Effects of Lactobacillus sakei inoculation on biogenic amines reduction and nitrite depletion of chili sauce

et al. 2022

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In this study, the effects of the starter culture Lactobacillus sakei on pH, the total lactic acid concentration, nitrite depletion and histamine reduction of chili sauce were investigated. The nitrite concentration in the CPN sample was significantly lower (p < 0.05) than that of the CPS sample (as control), and decreased by 30.87%.The putrescine and histamine concentration in starter culture inoculated chili sauce were significantly lower (p < 0.05) than that of the control sample, and were decreased by 38.08% and 49.88%, respectively. These results revealed that L. sakei could be used as a potential starter culture for nitrite depletion and biogenic amines reduction of chili sauce with good sensory attributes.

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Fibrinolytic bacteria of Indonesian fermented soybean: preliminary study on enzyme activity and protein profile

Abstract: A number of fibrinolytic enzyme producing microorganisms have been identified in various fermented food in Asia, such as from

Cited by 11 publications

References 46 publications

Molecular docking of Subtilisin K2, a fibrin-degrading enzyme from Indonesian moromi, with its substrates

Molecular docking of Subtilisin K2, a fibrin-degrading enzyme from Indonesian moromi, with its substrates

Role of Fibrinolytic Enzymes in Anti-Thrombosis Therapy

Effects of Lactobacillus sakei inoculation on biogenic amines reduction and nitrite depletion of chili sauce

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