Comparative characterization of two serine endopeptidases from Nocardiopsis sp. NCIM 5124

Dixit, Vaishali; Pant, Aditi

doi:10.1016/s0304-4165(00)00132-x

Cited by 25 publications

(8 citation statements)

References 30 publications

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“…Nocardiopsis NCIM 5124 isolated from an oil-polluted tropical marine environment near Mumbai, India (Dixit and Pant 2000a) and recently identified as N. dassonvillei on the basis of 16 s rDNA sequence similarities (unpublished results) also produced two types of alkaline serine endopeptidases referred to as proteases I and II (Dixit and Pant 2000b). Both the alkaline proteases demonstrated collagenolytic and fibrinolytic activities, and protease I could also degrade elastin.…”

Section: Features Of Proteases Produced By Nocardiopsis Speciesmentioning

confidence: 93%

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Bennur

Kumar

Zinjarde

et al. 2014

Appl Microbiol Biotechnol

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Members of the genus Nocardiopsis are generally encountered in locations that are inherently extreme. They are present in frozen soils, desert sand, compost, saline or hypersaline habitats (marine systems, salterns and soils) and alkaline places (slag dumps, lake soils and sediments). In order to survive under these severe conditions, they produce novel and diverse enzymes that allow them to utilize the available nutrients and to thrive. The members of this genus are multifaceted and release an assortment of extracellular hydrolytic enzymes. They produce enzymes that are cold-adapted (α-amylases), thermotolerant (α-amylases and xylanases), thermoalkalotolerant (cellulases, β-1,3-glucanases), alkali-tolerant thermostable (inulinases), acid-stable (keratinase) and alkalophilic (serine proteases). Some of the enzymes derived from Nocardiopsis species act on insoluble polymers such as glucans (pachyman and curdlan), keratin (feathers and prion proteins) and polyhydroxyalkanoates. Extreme tolerance exhibited by proteases has been attributed to the presence of some amino acids (Asn and Pro) in loop structures, relocation of multiple salt bridges to outer regions of the protein or the presence of a distinct polyproline II helix. The range of novel enzymes is projected to increase in the forthcoming years, as new isolates are being continually reported, and the development of processes involving such enzymes is envisaged in the future.

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Section: Features Of Proteases Produced By Nocardiopsis Speciesmentioning

confidence: 93%

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Bennur

Kumar

Zinjarde

et al. 2014

Appl Microbiol Biotechnol

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“…Recently, alkaline protease from Nocardiopsis sp. NCIM 5124 (8) has been purified and characterized. Similarly, an alkaline protease was purified and crystallized from Nesterenkoni sp.…”

Section: Introductionmentioning

confidence: 99%

Secretion of an alkaline protease from a salt- tolerant and alkaliphilic, Streptomyces clavuligerus strain Mit-1

Thumar

Singh

2007

Braz. J. Microbiol.

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An alkaliphilic and salt-tolerant actinomycete, Streptomyces clavuligerus strain Mit-1, was isolated from Mithapur, the western coast of India. The organism was Gram-positive, having filamentous, long thread like structure. The sporulation started after two days of growth and the optimum level of alkaline protease (130 U/ ml) was produced during the early stationary phase. The strain could grow and produce protease with 0-10% NaCl (w/v), the optimum being 5% NaCl (w/v). Growth and protease production was optimum at pH 9 with substantial decline at neutral pH. Sucrose and gelatin were the best carbon and nitrogen sources respectively, whereas gelatin broth was the preferred medium for protease production. Mit-1 produced substantial protease with various amino acids, when employed as the sole nitrogen sources. Crude substrates, such as molasses, whey and wheat flour had significant effect on enzyme production. The results are quite valuable, as only few actinomycetes, particularly salt-tolerant alkaliphilic ones, have so far been explored for their enzymatic potential and process optimization.

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“…594; Mitsuiki et al (2002) for Nocardiopsis sp. TOA-1 and Dixit & Pant (2000) for Nocardiopsis sp. NCIM 5124.…”

Section: Resultsmentioning

confidence: 99%

Production and Optimization of Alkaline Protease in Submerged Fermentation by Streptomyces rochei NRC 24

2012

Egypt. J. Microbiol.

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Streptomyces rochei NRC 24, under submerged fermentation (SF) conditions. The isolate exhibited maximum enzyme production with fermentation medium composed of peptone, glucose, K 2 HPO 4 , MgSO 4 .7H 2 O, NaCl, and CaCl 2. The studies on environmental parameters revealed that maximum level of alkaline protease production (220.92 U/ml) was achieved during stationary phase of S. rochei NRC 24 with optimum initial pH 9, inoculum size of 2% from stock spore suspension (5.6 x 10 6 spores/ml), and with a culture volume of 75 ml in 250 ml Erlenmeyer flasks under shaking conditions of 200 rpm. Of different nitrogen sources, casein and peptone with 0.4% of each proved to achieve maximum level of enzyme production. Screening experiments on medium components showed that the presence of peptone, glucose, MgSO 4 .7H 2 O, NaCl and CaCl 2 were essential for alkaline protease production. The absence of K 2 HPO 4 from the medium did not totally influence the enzyme production. Based on these results, De Meo's fractional factorial design was applied to find out the optimal conditions for maximal alkaline protease production. Optimization of the medium was carried out in three steps and Streptomyces rochei NRC 24 grew in the optimized medium producing 555.61 U/ ml compared to the growth of the strain on the basal medium before optimization (224 U/ ml).

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Comparative characterization of two serine endopeptidases from Nocardiopsis sp. NCIM 5124

Cited by 25 publications

References 30 publications

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Secretion of an alkaline protease from a salt- tolerant and alkaliphilic, Streptomyces clavuligerus strain Mit-1

Production and Optimization of Alkaline Protease in Submerged Fermentation by Streptomyces rochei NRC 24

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