Characterization of an Intracellular Alkaline Serine Protease from Bacillus velezensis SW5 with Fibrinolytic Activity

Yang, H. N.; Liu, Yang; Ning, Yuchang; Wang, Changyu; Zhang, Xin; Weng, Peifang; Wu, Zufang

doi:10.1007/s00284-020-01977-6

Cited by 19 publications

(22 citation statements)

References 37 publications

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“…The molecular mass of Velefibrinase was lower than that of many other fibrinolytic enzymes, such as Brevithrombolase (56 KDa) [ 32 ] and Russelobin (51.3 KDa) [ 27 ], but also higher than that of several fibrinolytic enzymes such as PAIEM (14.9 KDa) [ 33 ] and C142 (23.5 KDa) [ 34 ]. Moreover, Velefibrinase belonged to the peptidase S8 family (subtilisin family, clan SB), which is similar to other fibrinolytic enzymes purified from B. velezensis SW5 [ 18 ].…”

Section: Discussionmentioning

confidence: 99%

“…Data on Bacillus velezensis have been applied widely to the field of biological control and promotion of plant growth [ 13 ] and have shown its potential as a probiotic [ 14 ]. However, several studies only reported the discovery of and cloned fibrinolytic enzyme in Bacillus velezensis [ 15 , 16 , 17 , 18 ], therefore, it is a topic of further research. In the present study, a fibrinolytic protease (named Velefibrinase) was purified from marine B. velezensis Z01, which was screened from sea mud and its biochemical property was characterized.…”

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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Fibrinolytic enzymes are the most effective agents for the treatment of thrombotic diseases. In the present study, we purified and characterized an extracellular fibrinolytic serine metalloprotease (named Velefibrinase) that is produced by marine Bacillus velezensis Z01 and assessed its thrombolysis in vivo. SDS-PAGE and MALDI-TOF-MS analyses showed that the molecular mass of Velefibrinase was 32.3 KDa and belonged to the peptidase S8 family. The optimal fibrinolytic activity conditions of Velefibrinase were 40 °C and pH 7.0. Moreover, Velefibrinase exhibited high substrate specificity to fibrin, and a higher ratio of fibrinolytic/caseinolytic (1.48) values, which indicated that Velefibrinase had excellent fibrinolytic properties. Based on the degradation pattern of fibrin and fibrinogen, Velefibrinase could be classified as α/β-fibrinogenase. In vitro, Velefibrinase demonstrated efficient thrombolytic ability, anti-platelet aggregation, and amelioration of blood coagulation (APTT, PT, TT, and FIB), which were superior to those of commercial anticoagulant urokinase. Velefibrinase showed no hemolysis for erythrocyte in vitro and no hemorrhagic activity in vivo. Finally, Velefibrinase effectively prevented mouse tail thrombosis in a dose-dependent (0.22–0.88 mg/kg) manner. These findings suggested that Velefibrinase has the potential to becoming a new thrombolytic agent.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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“…Protease from viral, fungal, plant and animal origins has received a great deal of interest in recent years for the synthesis of many small peptides, especially dipeptides and tripeptides utilizing either a thermodynamically or a kinetically controlled bioprocess. (Kumar and Bhalla 2005 ; Motyan et al 2013 ; Yang et al 2020 ). Organic solvent-tolerant alkaline proteases from the genera Aspergillus, Bacillus, and Pseudomonas have shown promise for peptide synthesis (Song et al 2020 ).…”

Section: Microbial Proteases and Its Industrial Applicationsmentioning

confidence: 99%

“…The influence of a supplemental dietary mixture of different proteases in granular form cysteine protease and a serine endopeptidase on the productivity variables in dairy cattle, using as a model lactating Holstein cows was studied by Park et al ( 2020 ). The outcome of the experiment showed that supplemental protease enhances milk and meat production effectiveness and enhances parameters of nitrogen status (Yang et al 2020 ). A novel serine protease, expressed in Bacillus licheniformis as feed protease, permitted a significant augmentation in the degree of the hydrolysis, solubilization, and digestibility of proteins, improving broiler performance by enhancing protein and energy digestibility (Naveed et al 2021 ).…”

Section: Microbial Proteases and Its Industrial Applicationsmentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Putatunda²,

et al. 2021

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Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

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“…B. velezensis is potential starter culture of fermented foods (Cho et al., 2018 ). Recently, B. velezensis BS2 from a traditional Korean fermented seafood and B. velezensis SW5 from fish sauce showed fibrinolytic activity (Yang et al., 2020 ; Yao et al., 2019 ). A novel fermented soybean food by various microbes ( B. subtilis GD 1, B. subtilis N4, B. velezensis GZ1, L. bulgaricus , and H. anomala CICC 1728) showed peptide, total phenol, total flavonoid contents, suitable organic acid and biological amine contents, strong antioxidant and antifatigue activities (Cui et al., 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Novel green soybean shuidouchi fermented by Bacillus velezensis with multibioactivities

Hong

Luo

Liu

et al. 2021

Food Science & Nutrition

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Douchi, a traditional soybean food in China, has often been consumed as delicious condiment with functional effects (Wang et al., 2021). Shuidouchi is a typical bacteria-fermented douchi, which has a history of seasoning or dish for thousands of years.The product is in a wet state with a high water content (Luo et al., 2010). The fermentation process of shuidouchi includes two stages: (1) soaked and cooked soybeans are prefermented by microorganisms until viscin threads produced among soybeans, and (2) sterile water and some auxiliary materials such as salt, pepper powder, and other species are added to the prefermented

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Characterization of an Intracellular Alkaline Serine Protease from Bacillus velezensis SW5 with Fibrinolytic Activity

Cited by 19 publications

References 37 publications

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Microbial proteases: ubiquitous enzymes with innumerable uses

Novel green soybean shuidouchi fermented by Bacillus velezensis with multibioactivities

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