Production, purification, and functional properties of microbial fibrinolytic enzymes produced by microorganism obtained from soy-based fermented foods: developments and challenges

Yao, Mingjing; Yang, Yang; Fan, Jing; Ma, Chunmin; Liu, Xiaofei; Wang, Yan; Wang, Bing; Sun, Zhihui; McClements, David Julian; Zhang, Jiaxiang; Liu, Liping; Xia, Guanghua; Zhang, Na; Sun, Quancai

doi:10.1080/10408398.2022.2134980

Cited by 5 publications

(1 citation statement)

References 181 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Serine proteinase plasmin, a group of plasmin with a serine in its core catalytic domain by catalyzing the fibrin degradation process of fibrin clots [83]. Compared with the metalloprotease plasmin, serine proteinase plasmin is ineffective when administered by the intravenous route because it is rapidly neutralized by plasma antiplasmin [84].…”

Section: Serine Proteinase Plasmin-induced Hemorrhagementioning

confidence: 99%

Fibrinolytic drugs induced hemorrhage: mechanisms and solutions

Tang

Lin

et al. 2023

Blood Coagulation &Amp; Fibrinolysis

View full text Add to dashboard Cite

Thrombosis has been emerging as a major global life-threatening issue with high mortality and serious complications, especially in the post-COVID-19 era. Compared with the commonly used plasminogen activators thrombolytic drugs, fibrinolytic drugs are no longer heavily dependent on the patients’ own plasminogen, which are poorly expressed in most patients. As a novel “direct acting” thrombolytic agent, fibrinolytic drugs are considered to have stronger thrombolytic efficacy and safety than the widely used plasminogen activators. However, the risk of their hemorrhage remains a major concern. Herein, the molecular mechanisms and solutions were summarized for the first time based on the systematic review of the latest developments, which could shed new light on the development of novel safety fibrinolytic drugs in the future.

show abstract

Section: Serine Proteinase Plasmin-induced Hemorrhagementioning

confidence: 99%

Fibrinolytic drugs induced hemorrhage: mechanisms and solutions

Tang

Lin

et al. 2023

Blood Coagulation &Amp; Fibrinolysis

View full text Add to dashboard Cite

show abstract

Therapeutic and Anti-Thrombotic Properties of Some Naturally Fermented Soybean Foods of the Eastern Himalayas

2023

View full text Add to dashboard Cite

Naturally fermented soybean foods have anti-thrombotic properties due to the presence of microbial fibrinolytic enzymes. However, fibrinolytic enzyme-producing bacteria from naturally fermented soybean foods of the Eastern Himalayas viz. kinema, grep-chhurpi, peha, peron namsing, peruñyaan and bemerthu have not been screened yet. Therefore, this study aims to screen the fibrinolytic enzyme-producing bacteria from these naturally fermented soybean foods and also to assess their therapeutic properties such as antioxidant, anti-inflammatory, flavones, isoflavones, anti-obesity and anti-diabetic properties of samples. A total of 877 bacteria were isolated, out of which Bacillus subtilis (ten strains), B. velezensis (three strains), B. inaquosorum (two strains) and B. halotolerans (one strain) showed fibrinolytic enzyme activity ranging from 775.70 U/mL to 1230.61 U/mL, with a blood clot-degrading property of more than 50%. A remarkable DPPH radical scavenging property (>50%), flavone (278.98 ± 7.06 µg QE/g) and isoflavone (394.13 ± 11.68 µg GEN/g) contents were observed. The Himalayan fermented soybean foods have shown anti-thrombotic, antioxidant, anti-inflammatory, anti-diabetic and anti-obesity properties indicating their therapeutic values.

show abstract

Isolation and Optimal Fermentation Conditions of Bacillus licheniformis SFD-Y5 for a New Douchi Fibrinolytic Enzyme Producer

Yao

Bian

et al. 2023

Fermentation

View full text Add to dashboard Cite

Cardiovascular disease (CVD) has become the leading cause of death, and it is critical to develop new functional foods to prevent intravascular thrombosis, the key cause of CVD. Fermented soy-based food is a good choice because of its native fibrinolytic enzyme (FE) activity. In this study, a strain that can produce a new type of fibrinolytic enzyme was selected from Chinese Douchi and identified as Bacillus licheniformis SFD-Y5 by molecular biology experiments and physiological and biochemical experiments. Single factor experiments combined with statistical experiments, including Plackett–Burman experiment, steepest ascent experiment and RSM (Box–Behnken design), were used to optimize the fermentation of FE by B. licheniformis SFD-Y5. The final FE activity was 2434.45 ± 28.49 IU/mL under optimal conditions, which is the highest FE activity produced by wild B. licheniformis so far. Further studies showed that Y5 FE is a serine metalloproteinase with good stability at alkaline pHs (pH 8.0–11.0). The results of our study could lay a foundation for the future production, molecular modification and further application in functional foods of Y5 FE.

show abstract

Production, purification, and functional properties of microbial fibrinolytic enzymes produced by microorganism obtained from soy-based fermented foods: developments and challenges

Cited by 5 publications

References 181 publications

Fibrinolytic drugs induced hemorrhage: mechanisms and solutions

Fibrinolytic drugs induced hemorrhage: mechanisms and solutions

Therapeutic and Anti-Thrombotic Properties of Some Naturally Fermented Soybean Foods of the Eastern Himalayas

Isolation and Optimal Fermentation Conditions of Bacillus licheniformis SFD-Y5 for a New Douchi Fibrinolytic Enzyme Producer

Contact Info

Product

Resources

About