Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007

Wang, San-Lang; Ying, Wei; Liang, Tzu Wen

doi:10.1016/j.nbt.2010.09.003

Cited by 72 publications

(52 citation statements)

References 28 publications

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“…The fibrinolytic activity was determined using the spectrophotometric method described by Wang et al [18]. First, 0.4 mL of 0.72% fibrinogen was placed in a test tube with 0.1 mL of 245 mM phosphate buffer (pH 7) and incubated at 37˚C for 5 min.…”

Section: Fibrinolytic Activitymentioning

confidence: 99%

Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation

Nascimento¹,

Sales²,

Porto³

et al. 2015

AER

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Fibrinolytic enzymes have received attention regarding their medicinal potential for thrombolytic diseases, a leading cause of morbidity and mortality worldwide. Various natural enzymes purified from animal, plant and microbial sources have been extensively studied. The aim of this work was to produce fibrinolytic protease by solid state fermentation using agro industrial substrates. Rhizopus arrhizus var. arrhizus UCP 1295 and Mucor subtillissimus UCP 1262 filamentous fungi species isolated from soil of Caatinga-PE, Brasil, were used as producer microorganisms. Wheat bran was shown to be the best substrate for the production of the enzyme and by using a 2 3 full factorial design the main effects and interactions of the quantity of the substrate wheat bran, moisture and temperature on the fibrinolytic enzyme production and protease were evaluated. The best results for fibrinolytic and protease activities, 144.58 U/mL and 48.33 U/mL, respectively, were obtained with Mucor subtillissimus UCP 1262 using as culture medium 3 g wheat bran, 50% moisture at a temperature of 25˚C for 72 hours. The optimum temperature for the produced enzyme was 45˚C and most of its original activity was retained after being subjected to 80˚C for 120 min. The pro-* Corresponding author.T. P. Nascimento et al. 82tease activity was enhanced by K + , Ca + and Mn + ; but with Cu + there was an inhibition. The specificity to chromogenic substrate and the inhibition by PMSF indicates that it is a chymotrypsin-like serine protease. Presented results suggest that this enzyme produced by solid-state fermentation is an interesting alternative as a candidate for thrombolytic therapy.

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Section: Fibrinolytic Activitymentioning

confidence: 99%

Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation

Nascimento¹,

Sales²,

Porto³

et al. 2015

AER

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“…Two keratinases produced by B. licheniformis PWD-1, i.e. Versazyme and Cibenza DP100, have shown excellent results in broiler performance and growth of piglets (Odetallah et al 2005;Wang et al 2011).…”

Section: Proteases For Processing Of Keratin Wastesmentioning

confidence: 99%

“…Proteases may have application potential for production of shrink-proof wool in an environmentally friendly process. However, protease treatment in general damages the wool by causing excessive loss of strength, and lowering the antifelting ability, which in turn may lead to additional damage to the fibre interior during wool processing (Wang et al 2011). Therefore, specific proteases whose action is limited to cuticle scale of wool fibre are desired (Shen et al 2007).…”

Section: Proteases For Biopolishing Of Woolmentioning

confidence: 99%

Potential application spectrum of microbial proteases for clean and green industrial production

Singh

Bajaj

2017

Energ. Ecol. Environ.

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Enzymes are the cornerstones of metabolism and constitute the fundamental basis for existence of life. However, recently enzymes are being implicated in diverse industrial processes because of their specific and fast action for efficient bioconversion of substrate to product, and their capability to save raw materials, energy and chemicals for various manufacturing processes. Enzymes are considered as environment-friendly (green) chemicals that may potentially help replacing completely or reducing the usage of hazardous chemicals for industrial processes, thus promising sustainable production and manufacturing. Among various industrial enzymes microbial proteases dominate the world enzyme market due to their multifaceted application potential in varied bioindustries like food, pharmaceutical, textile, photographic, leather and detergent. Promising applications of proteases in agricultural sector for instance may include biocontrol of pests, degumming of silk, selective delignification of hemp and wool processing. However, for successful industrial applications the proteases must be robust enough to suit the process conditions which are generally hostile. Proteases intended for industrial applications must have activity and stability over wide range of temperature and pH extremes for prolonged time periods and even in the presence of various potential enzyme inhibitors. Of various microbial proteases those from Bacillus spp. have got special significance because the latter are known for their ability to produce sturdy enzymes that might have suitability for industrial process conditions. The current article presents an interpretive summary of the recent developments on application potential of proteases for various industries.

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“…TKU015 and B. subtilis TKU007 are able to produce NK using shrimp shell wastes as the sole carbon/ nitrogen source. Shrimp shell powder is a fishery waste; thus, the production procedure using this substrate would be very cost effective and favors producing inexpensive fibrinolytic enzymes (Wang et al 2009c(Wang et al , 2011. Fibrinogen and fibrin have also been used as substrates in culture media for NK production.…”

Section: Nattokinase Production and Formulationmentioning

confidence: 99%

Nattokinase: production and application

Dabbagh

Negahdaripour

Berenjian

et al. 2014

Appl Microbiol Biotechnol

103

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Nattokinase (NK, also known as subtilisin NAT) (EC 3.4.21.62) is one of the most considerable extracellular enzymes produced by Bacillus subtilis natto. The main interest about this enzyme is due to its direct fibrinolytic activity. Being stable enough in the gastrointestinal tract makes this enzyme a useful agent for the oral thrombolytic therapy. Thus, NK is regarded as a valuable dietary supplement or nutraceutical. Proven safety and ease of mass production are other advantages of this enzyme. In addition to these valuable advantages, there are other applications attributed to NK including treatment of hypertension, Alzheimer's disease, and vitreoretinal disorders. This review tends to bring a brief description about this valuable enzyme and summarizes the various biotechnological approaches used in its production, recovery, and purification. Some of the most important applications of NK, as well as its future prospects, are also discussed.

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Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007

Cited by 72 publications

References 28 publications

Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation

Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation

Potential application spectrum of microbial proteases for clean and green industrial production

Nattokinase: production and application

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Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007

Cited by 72 publications

References 28 publications

Production and Characterization of New Fibrinolytic Protease from &lt;i&gt;Mucor subtillissimus&lt;/i&gt; UCP 1262 in Solid-State Fermentation

Production and Characterization of New Fibrinolytic Protease from &lt;i&gt;Mucor subtillissimus&lt;/i&gt; UCP 1262 in Solid-State Fermentation

Potential application spectrum of microbial proteases for clean and green industrial production

Nattokinase: production and application

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Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation

Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation