Characterisation of acid protease expressed from Aspergillus oryzae MTCC 5341

Vishwanatha, K. S.; Rao, A. G. Appu; Singh, Sridevi Annapurna

doi:10.1016/j.foodchem.2008.09.070

Cited by 102 publications

(98 citation statements)

References 27 publications

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“…The observed half-life for the protease was approximately 120 minutes at 50°C. The thermostability of acidic proteases highly varied within the Rhizopus oryzae (30-45°C) [11], Aspergillus oryzae MTCC 5341 (40-57°C) [30], A. niger I1 (30-40°C) [3], and Mucor pilosus (25-55°C) [31] species. Rhizopuspepsin from R. oryzae MTCC 3690 had a half-life of ~20 minutes at 60°C, and retained full activity after Fig.…”

Section: Results and Disscusionmentioning

confidence: 99%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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Abstract:The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50℃. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50℃, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na . It was proposed that the studied acidic protease might represent a previously uncharacterised type of acidic protease produced by the Rhizopus stolonifer RN-11 strain.

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Section: Results and Disscusionmentioning

confidence: 99%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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“…As a part of purification and characterization of proteases from A. oryzae MTCC 5341, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram confirm the release of one dominant acid protease [32]. The acid protease from A. oryzae MTCC 5341 has been purified with a yield of 29%, having a specific activity of 43,658 U/mg [32]. The enzyme prefers hydrophobic amino acids at S 1 and S 1 0 positions and also activates trypsinogen to trypsin [32].…”

Section: Introductionmentioning

confidence: 99%

Acid protease production by solid-state fermentation using Aspergillus oryzae MTCC 5341: optimization of process parameters

Vishwanatha¹,

Rao²,

Singh³

2009

J Ind Microbiol Biotechnol

116

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Aspergillus oryzae MTCC 5341, when grown on wheat bran as substrate, produces several extracellular acid proteases. Production of the major acid protease (constituting 34% of the total) by solid-state fermentation is optimized. Optimum operating conditions obtained are determined as pH 5, temperature of incubation of 30 degrees C, defatted soy flour addition of 4%, and fermentation time of 120 h, resulting in acid protease production of 8.64 x 10(5) U/g bran. Response-surface methodology is used to generate a predictive model of the combined effects of independent variables such as, pH, temperature, defatted soy flour addition, and fermentation time. The statistical design indicates that all four independent variables have significant effects on acid protease production. Optimum factor levels are pH 5.4, incubation temperature of 31 degrees C, 4.4% defatted soy flour addition, and fermentation time of 123 h to yield a maximum activity of 8.93 x 10(5) U/g bran. Evaluation experiments, carried out to verify the predictions, reveal that A. oryzae produces 8.47 x 10(5) U/g bran, which corresponds to 94.8% of the predicted value. This is the highest acid protease activity reported so far, wherein the fungus produces four times higher activity than previously reported [J Bacteriol 130(1): 48-56, 1977].

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“…Study by Anandan et al [26] has shown that when added wheat bran in media containing glucose and other nutrients sources, such as citrate, maltose, lactose and sucrose, Aspergillus tamarii NRRL20818showed excellent proteolytic activities. In another study with Aspergillus oryzae MTCC5341 and using rice bran and wheat bran as substrates, the last one increased the proteolytic activity of 25.6% compared with rice bran [7]. …”

Section: Screening Of Aspergillus For Protease Productionmentioning

confidence: 97%

“…Some strains from Aspergillus genus are considered non-toxic, recognized as a safe microorganism by the Food and Drug Administration (FDA), denominated Generally Recognized as Safe (GRAS), and used for human and animal nutrition [5] [6] [7].…”

Section: Introductionmentioning

confidence: 99%

“…The combination of the microbial cell and different substrates comprises metabolic and biotransformation process that can generate several cellular products. Additionally, the microorganism and substrate selection plus the biochemical characteristic of the enzyme produced are important factors to evaluate its biotechnological potential and target the possible applications for industrial processes [5] [6] [7] [8]. The aim of this study was to produce in different agroindustrial substrates and characterize extracellular protease from Aspergillus tamarii URM4634 by Solid-state Fermentation.…”

Section: Introductionmentioning

confidence: 99%

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Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

Silva¹,

Oliveira²,

Souza-Motta³

et al. 2016

AER

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This study reports the protease production from Aspergillus tamarii using agroindustrial residues as substrate for solid-state fermentation (SSF) and biochemical characterization. The highest protease production was obtained using wheat bran as substrate at 72 h fermentation with maximum proteolytic activity of 401.42 U/mL, collagenase of 243.0 U/mL and keratinase of 19.1 U/mL. The protease exhibited K M = 18.7 mg/mL and Vmax = 28.5 mg/mL/min. The optimal pH was 8.0 and stable in a wide pH range (5.0 -11.0) during 24 h. The optimum temperature was 40˚C. The proteolytic activity was inhibited by Cu 2+ (33.98%) and Hg 2+ (22.69%). The enzyme was also inhibited by PMSF (65.11%), indicating that is a Serine Protease. These properties suggest that alkaline protease from A. tamarii URM4634 is suitable for application in food industries and leather processing. Additionally, the present findings opened new vistas in the utilization of wheat bran and other effective agroindustrial wastes as substrates for SSF.

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Characterisation of acid protease expressed from Aspergillus oryzae MTCC 5341

Cited by 102 publications

References 27 publications

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Acid protease production by solid-state fermentation using Aspergillus oryzae MTCC 5341: optimization of process parameters

Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

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Characterisation of acid protease expressed from Aspergillus oryzae MTCC 5341

Cited by 102 publications

References 27 publications

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Acid protease production by solid-state fermentation using Aspergillus oryzae MTCC 5341: optimization of process parameters

Novel Protease from &lt;i&gt;Aspergillus tamarii&lt;/i&gt; URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

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Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation