Production of a collagenase from Candida albicans URM3622

Lima, Carolina de Albuquerque; Rodrigues, P; Porto, Tatiana Souza; Viana, Daniela; Filho, J. L. Lima; Cunha, Mariana

doi:10.1016/j.bej.2008.10.014

Cited by 41 publications

(53 citation statements)

References 33 publications

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“…Only the enzyme produced by Rhizoctonia solani was produced under acid pH (5.0) [14]. The results described at present work are in agreement with those reported in literature that show that collagenases exhibit optimum activity values under neutral or alkaline conditions [23,39]. These results indicate that this collagenolytic enzyme belongs to the group of alkaline proteases.…”

Section: Effect Of Ph On Collagenolytic Activity and Stabilitysupporting

confidence: 91%

“…UCP 1286. The literature describes the importance of defining parameters that have a significant influence on the extracellular enzyme production by microorganisms -not only the composition of the culture medium as a carbon and nitrogen sources and trace elements should be considered but also the culture conditions such as pH, temperature and stirring speed [23]. Present work Ac = collagenolytic activity (U/mL), *Specific activity (U/mg), N.I.…”

Section: Enzyme Production Kineticsmentioning

confidence: 99%

“…According to Jain and Jain [1], the maximum production obtained for Streptomyces exfoliates (43.5 U/mL) was observed after 5 days of culture at 30 °C and 150 rpm. Lima et al [23] conducted a 2 3 full factorial for the production of collagenase with Candida albicans and found the highest value (7.6 U/mL) with a 2% substrate concentration, agitation of 160 rpm and pH 7.0. For Penicillium aurantiogriseum, Lima et al [9] reported that the of fermentation.…”

Section: 4 Factorial Designmentioning

confidence: 99%

“…Studies have reported the biosynthesis of collagenases by fungi belonging to the different genera, such as Aspergillus, Cladosporium, Alternaria, Penicillium [8,[20][21][22], Candida [23], Microsporum [24] and Rhizoctonia [14]. Species of Penicillium genus have a higher biotechnological potential compared to other genera cited, both for production of proteases and other enzymes, as they have the capacity of growth in different culture conditions, using a wide variety of substrates as nutrients [25].…”

Section: Introductionmentioning

confidence: 99%

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Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

2016

J App Biol Biotech

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A new Penicillium sp. strain isolated from the soil of Caatinga, a Brazilian Biome (UCP 1286) was selected for collagenase production. Fermentation system allowing obtention of collagenolytic activity about 2.7 times higher than existing data, with the highest values of collagenolytic and specific activity (379.80 U/mL, 1460.77 U/mg, respectively), after 126 hours. Applying a factorial design, enzyme production was increased by about 65% compared to the preliminary results. The factorial design demonstrated the existence of two factors with statistical significance on the production of the enzyme: pH and temperature, both with negative effects. Enzyme was found to be more active at pH 9.0 and 37 °C, and also to be very stable in comparison with the collagenase produced by other microorganisms. The enzyme seems to belong to collagenolytic serine proteases family. Concerning the substrate specificity, it was observed that the highest enzyme activity corresponds to azocoll, there was no relevant activity on azocasein and the enzyme showed to be more specific to type V collagen and gelatin than the commercial colagenase produced by Clostridium histolyticum. Major band observed at electrophoresis was approximately 37 kDa. Zymogram analysis confirmed the collagenolytic activity. All data indicates this enzyme as promising biotechnology product.

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Section: Effect Of Ph On Collagenolytic Activity and Stabilitysupporting

confidence: 91%

Section: Enzyme Production Kineticsmentioning

confidence: 99%

Section: 4 Factorial Designmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

2016

J App Biol Biotech

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“…Following the cultivation of the microorganism the enzymatic activity was 7.2 U mL -1 and the specific activity was 10 U mg -1 . The result of the present study was close to that obtained by Lima et al, 35 in the production of collagenase enzyme by Candida albicans, which had a value of 7.06 U mL -1 . Nakayama et al, 36 studied the production of collagenase enzyme by Bacillus NATP-1, previously described as A. sendaiensis, 4 and obtained enzymatic activity of 24 U mL -1 through the use of oxygen and pH control during enzyme production in a potato dextrose broth medium.…”

Section: Production Of Collagenase By Alicyclobacillus Sendaiensis Kcsupporting

confidence: 79%

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

et al. 2017

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The biosynthesis of amylase and collagenase, produced by A. acidocaldarius and A. sendaiensis respectively, were studied, and different matrices evaluated for the microorganisms immobilization and enzymes production optimization, such as loofa sponge, alginate-sponge and alginate, followed by concentration through ultrafiltration. Using a wheat bran substrate, the amylase enzyme displayed enzymatic activity of 0.45 U mL -1 and optimum temperature and pH conditions of 75 °C and pH 3.0, respectively. Thermal stability was in the range of 55 to 60 °C. The apparent Km and Vmax were 3.2 mg mL -1 and 0.5 U mL -1, respectively. The production of collagenase by A. sendaiensis was carried out with potato dextrose broth substrate and the activity obtained was 7.2 U mL -1 . For amylase, the best results were obtained from immobilization in loofa sponge and the use of ultrafiltration (0.67 U mL -1) and for the collagenase extract, from the free biomass and ultrafiltration (13.6 U mL -1 ). The use of an ultrafiltration system enabled an average increase of 54% in the activity of both enzymes. Therefore, Alicyclobacillus are capable of producing enzymes of industrial interest, with the possibility of economically viable application of the substrate, and the use of immobilization and ultrafiltration produced positive results.

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Polymer‐based alternative method to extract bromelain from pineapple peel waste

Novaes

Santos-Ebinuma

Mazzola

et al. 2013

Biotech and App Biochem

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Bromelain is a mixture of proteolytic enzymes present in all tissues of the pineapple (Ananas comosus Merr.), and it is known for its clinical therapeutic applications, food processing, and as a dietary supplement. The use of pineapple waste for bromelain extraction is interesting from both an environmental and a commercial point of view, because the protease has relevant clinical potential. We aimed to study the optimization of bromelain extraction from pineapple waste, using the aqueous two-phase system formed by polyethylene glycol (PEG) and poly(acrylic acid). In this work, bromelain partitioned preferentially to the top/PEG-rich phase and, in the best condition, achieved a yield of 335.27% with a purification factor of 25.78. The statistical analysis showed that all variables analyzed were significant to the process.

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Production of a collagenase from Candida albicans URM3622

Cited by 41 publications

References 33 publications

Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

Polymer‐based alternative method to extract bromelain from pineapple peel waste

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