Production and characterization of a collagenolytic serine proteinase by Penicillium aurantiogriseum URM 4622: A factorial study

Lima, Carolina de Albuquerque; Filho, J. L. Lima; Neto, B.B.; Converti, Attílio; Cunha, Mariana; Porto, Ana Lúcia Figueiredo

doi:10.1007/s12257-010-0247-0

Cited by 33 publications

(57 citation statements)

References 54 publications

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“…The results described in this paper show that the concentration of substrate (0.25%) used for the maximum production of collagenolytic enzyme (632.70 U/mL) was lower than those reported in the literature, which can represent an economy in production. With respect to the agitation, the results were similar to those related by Lima et al [9] (200 rpm). Temperature found in present work was lower than others papers (24 °C), and pH was slightly higher (9.0) showing that maximum enzyme production conditions are milder than those reported.…”

Section: 4 Factorial Designsupporting

confidence: 90%

“…Temperature is an important factor in regulating enzymatic synthesis [38]. In a study reporting the production of collagenase by Penicillium aurantiogriseum, the temperature also had a negative effect [9]. Since the initial pH of the culture medium influences many enzymatic processes, enzyme production, cell transport across membranes and expression of extracellular proteases, we observed, a gradual decrease in collagenase production when the external pH was raised from 6 to 8.…”

Section: 4 Factorial Designmentioning

confidence: 73%

“…Jain and Jain [1] showed that the maximum collagenase production (43.50 U/mL) was observed with higher biomass concentration (5.60 cm 3 of cells). The initial pH of the medium was shown by Lima et al [9] to be the factor that exhibited a significantly higher effect on the biomass, with an increase in pH causing a decrease in cell growth.…”

Section: 4 Factorial Designmentioning

confidence: 99%

“…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. pH = initial pH of the medium; So = initial concentration of gelatin; T = temperature; X = biomass concentration; TP = total protein; Ac = volumetric collagenolytic activity; ac = specific collagenolytic activity.…”

Section: 4 Factorial Designmentioning

confidence: 99%

“…These enzymes can degrade native triple helix of collagen to small fragments and play an important role in connective tissue metabolism [7,8]. Collagenolytic enzymes are a kind of proteases that are related to various physiological and pathological processes and have several applications in industry, medicine and biotechnology [6,[9][10][11]. With biotechnology accelerated growth, applications of proteases have expanded to new areas such as clinical, medicinal and analytical chemistry [12].…”

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: 4 Factorial Designsupporting

confidence: 90%

Section: 4 Factorial Designmentioning

confidence: 73%

Section: 4 Factorial Designmentioning

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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Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Oliveira

Silva

Converti

et al. 2019

Biotechnology Progress

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This study reports on the biochemical characterization as well as the kinetic and thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase (FFase) with transfructosylating activity. Conditions for FFase activity were optimized by means of a central composite rotational design using pH and temperature as the independent variables, while residual activity tests carried out in the temperature range of 45–65°C enabled us to investigate FFase thermostability and estimate the kinetic and thermodynamic parameters of enzyme denaturation. Optimal conditions for sucrose hydrolysis and fructosyl transfer catalyzed by crude FFase were 50°C, and pH 6.0 and 7.4, respectively. The thermodynamic properties of irreversible enzyme inactivation were found to be activation energy of 293.1 kJ mol−1, and activation enthalpy, entropy, and Gibbs free energy in the ranges 290.3–290.4 kJ mol−1, 568.7–571.0 J mol−1 K−1, and 97.9–108.8 kJ mol−1, respectively. The results obtained in this study point out satisfactory enzyme activity and thermostability at temperatures commonly used for industrial fructo‐oligosaccharide (FOS) synthesis; therefore, this novel FFase appears to be a promising biocatalyst with great potential for long‐term FOS synthesis and invert sugar production. To the best of our knowledge, this is the first report on kinetic and thermodynamic parameters of an A. tamarii FFase.

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Screening and application of fungal proteases for goat casein hydrolysis towards the development of bioactive hydrolysates

et al. 2022

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Production and characterization of a collagenolytic serine proteinase by Penicillium aurantiogriseum URM 4622: A factorial study

Cited by 33 publications

References 54 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

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Screening and application of fungal proteases for goat casein hydrolysis towards the development of bioactive hydrolysates

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