Biochemical properties of a serine protease from<i>Aspergillus flavus</i>and application in dehairing

Franco, Daniel Guerra; Spalanzani, Regiane Nogueira; Lima, Emmly Ernesto de; Marchetti, Clarice Rossato; Silva, Patrícia Oliveira; Masui, Douglas Chodi; Giannesi, Giovana Cristina; Zanoelo, Fabiana Fonseca

doi:10.1080/10242422.2017.1322584

Cited by 10 publications

(5 citation statements)

References 38 publications

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“…6). Similar results were obtained by Franco et al (2017), where the highest value of enzyme activity was seen within the temperature range of 45 to 55 °C. Yadav et al (2011) reported the maximum enzyme activity of protease from A. flavus at 40 °C, whereas, a maximum activity was reported at 50 °C by experimenting with protease from A. flavus (Muthulakshmi et al 2011).…”

Section: Characterization Of Alkaline Protease From a Flavussupporting

confidence: 87%

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Production, purification, and characterization of alkaline protease from Aspergillus flavus and its compatibility with commercial detergents

Wajeeha

Asad

Mahmood

et al. 2020

BioRes

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Aspergillus flavus was used to produce alkaline protease. Solid state fermentation (SSF) strategy was adopted to explore the most favorable physical and nutritional conditions for enzyme production. Maximum production was achieved at pH 6.0 and a temperature of 30 °C after 84 h of growth period. For the optimization of the chemical parameters, different carbon and nitrogen sources were used including glucose, fructose, sucrose, ammonium sulphate, and urea. Maximum production was observed with 0.3% concentration of all the compounds. Ammonium sulphate salting out and gel chromatography was used to purify the enzyme. The enzyme was completely precipitated out at 80% saturation. The value of Vmax was 3.9 U/mL, while the value of Km was 1.9 mg/mL. The enzyme was tested for its compatibility with a few famous detergents available on the market. With the alkaline protease under study, the enzyme displayed a maximum retention of its activity i.e. 80.8% in the presence of commercial detergent Surf excel. The activity dropped down to 61.5% when the enzyme was allowed to work in the presence of another locally used detergent, i.e., Bonus. Protease production from A. flavus was carried out on rice bran and wheat bran and the wheat bran gave better results.

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Section: Characterization Of Alkaline Protease From a Flavussupporting

confidence: 87%

“…Enzymes are the catalysts that regulate many chemical reactions occurring in the living body and are called biocatalysts (Raimi et al 2011). Proteases are enzymes that promote the cleavage of peptide bonds through hydrolysis (Franco et al 2017). They can be acidic, neutral, or alkaline.…”

Section: Introductionmentioning

confidence: 99%

Production, purification, and characterization of alkaline protease from Aspergillus flavus and its compatibility with commercial detergents

Wajeeha

Asad

Mahmood

et al. 2020

BioRes

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“…The consequent unfolding or denaturation of the polypeptide chains is then accompanied by the rapid loss of catalytic activity (Paulines et al 2013). The optimal temperature for crude protease in this study is similar to serine proteases reported previously from Aspergillus clavus (Franco et al 2017). The higher optimal temperature was also reported for proteases produced by Botrytis cinerea (Abidi et al 2011).…”

Section: Characteristics Of the Crude Proteasesupporting

confidence: 84%

Optimization and Functional Properties of a Protease from a Fish Gut Isolate Pseudomonas sp. PD14 Grown on Fish Processing Wastes Substrate

Armada¹,

Simora²

2021

Philipp J Sci

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Extracellular protease production from Pseudomonas sp. PD14 isolated from the gut of rabbitfish, Siganus guttatus, was investigated using fish processing wastes as nitrogen source. Three types of fish processing by-products – namely, heads, bones, and viscera – from yellowstripe scad (Selaroides sp.) and Japanese halfbeak (Hyporhampus sajori), as well as trimmings and viscera from squid (Loligo sp.) were used. Among the fish waste preparations tested, Japanese halfbeak viscera (HV) flour (1.0%) supported the maximum protease production of 365.0 U/mg protein. Effects of media components on protease production in the optimized concentration of HV flour revealed that the protease enzyme can be optimally produced using maltose (0.50%) as a carbon source, at pH 8.0, and incubated for 48 h at 40 °C. Partial characterization of the crude enzyme supernatant showed that the optimum pH and temperature were 8.0 and 50 °C, respectively. Furthermore, the crude protease exhibited thermostability retaining 50% activity at 60 °C and fairly stable up to pH 11.0. Considering the high costs of industrial enzyme production, the use of fish processing wastes for protease production offers a promising future for enzyme biotechnology.

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“…have also been reported [9, 10, 11]. Extracellular alkaline proteases contribute to 25% of total microbial enzyme sales [12] encompassing widespread applications in industrial sectors such as laundry [13], leather [14], silk [15], pharmaceutical [16], nutrition [17], silver recovery [18] etc.…”

Section: Introductionmentioning

confidence: 99%

A novel thiol-dependent serine protease from Neocosmospora sp. N1

Matkawala

Nighojkar²,

Kumar

et al. 2019

Heliyon

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Alkaline proteases have several industrial applications. In the present study, newly isolated Neocosmospora sp. N1 was screened as hyper producer of serine protease. A multimeric protease of the fungus was purified to homogeneity till 96.78 fold purification with 22.51% recovery. The homogeneity of purified enzyme was checked by native PAGE and its molecular weight was found to be 198.03 kDa by MALDI-TOF. On SDS-PAGE analysis, enzyme was found to be a hetero oligomer of 17.66 kDa and 20.89 kDa subunits. The purified enzyme showed maximum activity with casein as substrate at 60 C and pH 8.5. The K m and V max values were found to be 0.015 mg/ml and 454.45 U/ml, respectively. The enzyme was completely inhibited by PMSF, while the activity was 40% enhanced using β-mercaptoethanol, suggesting that it is a thiol-dependent serine protease. The purified protease was active over an alkaline pH range from 7 to 12 and temperatures from 20 C to 60 C. The enzyme exhibited excellent stability, almost 100% towards organic solvents such as toluene, benzene and hexane, surfactants such as Triton X-100, Tween-20, Tween-80 and SDS, as well as commercial detergents. The significant properties of purified enzyme assure that it could be a potential candidate for commercial purposes.

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Biochemical properties of a serine protease fromAspergillus flavusand application in dehairing

Cited by 10 publications

References 38 publications

Production, purification, and characterization of alkaline protease from Aspergillus flavus and its compatibility with commercial detergents

Production, purification, and characterization of alkaline protease from Aspergillus flavus and its compatibility with commercial detergents

Optimization and Functional Properties of a Protease from a Fish Gut Isolate Pseudomonas sp. PD14 Grown on Fish Processing Wastes Substrate

A novel thiol-dependent serine protease from Neocosmospora sp. N1

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