Medium optimization of protease production by Brevibacterium linens DSM 20158, using statistical approach

Shabbiri, Khadija; Adnan, Ahmad; Jamil, Sania; Ahmad, Waqar; Noor, Bushra; Rafique, H.M.

doi:10.1590/s1517-83822012000300031

Cited by 21 publications

(7 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…(Bhattacharya et al 2011) and protease production by Brevibacterium linens (Shabbiri et al 2012). Statistical optimization of production of various enzymes of chitinolytic enzyme system was attempted by several workers (Vaidya et al 2003; Gohel et al 2005; Juarez-Jimenez et al 2008; Lopes et al 2008).…”

Section: Resultsmentioning

confidence: 99%

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

Pareek¹,

Ghosh²,

Singh³

et al. 2013

3 Biotech

View full text Add to dashboard Cite

Optimization of the fermentation conditions for chitin deacetylase (CDA) production by Penicillium oxalicum SAEM-51 was undertaken in the present study using central composite design (CCD) under submerged condition. CDA is widely employed for bio-catalytic conversion of chitin to chitosan. Chitosan is a biopolymer with immense commercial potential in diverse industrial sectors, viz. pharmaceutics, food, agriculture, water treatment, etc. CDA production was significantly affected by all the variables studied, viz. pH, temperature, inoculum age and size. The optimal conditions that stimulating maximal CDA production were found to be: pH, 7.9; temperature, 28 °C; inoculum age, 90 h, and 11 % inoculum size. Under these optimized conditions, the actual maximal CDA production was 623.57 ± 8.2 Ul−1, which was in good agreement with the values predicted by the quadratic model (648.24 Ul−1), confirming the validity of the model. Optimization of fermentation conditions through CCD had resulted into 1.4-fold enhancement in CDA productivity (Qp = 4.3264 Ul−1 h−1). Results of these experiments indicated that response surface methodology was proved to be a promising method for optimization of CDA production.

show abstract

Section: Resultsmentioning

confidence: 99%

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

Pareek¹,

Ghosh²,

Singh³

et al. 2013

3 Biotech

View full text Add to dashboard Cite

show abstract

“…The amount of substrate and moisture showed no effect on the production of proteases by Brevibacterium linens DSM 20158 were obtained at 30˚C [28]. Both of works showed that temperature at 30˚C was responsible for the higher activity values.…”

Section: Full Factorial Design For Protease Production From a Tamarimentioning

confidence: 91%

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

View full text Add to dashboard Cite

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.

show abstract

“…It was thus possible to increase enzyme activity by 2.35 times (134.94%) in optimal conditions when compared to the best conditions obtained in the factorial design. Shabbiri et al (2012), using Central Composite Design, there was a 2.0 times increase in the production of protease by Brevibacterium linens DSM 20158. Meena et al (2013), using Taguchi methodology with optimized conditions, the alkaline protease production by Pseudomonas aeruginosa increased by 1.29 time (28.8%) In contrast, during the production of protease by Exiguobacterium sp.…”

Section: Validationmentioning

confidence: 99%

Extracellular serine proteases by Acremonium sp. L1-4B isolated from Antarctica: Overproduction using cactus pear extract with response surface methodology

Nascimento

Sena

Gomes

et al. 2015

Biocatalysis and Agricultural Biotechnology

View full text Add to dashboard Cite

Acremonium sp. L1-4B isolated from lichen in Antarctica was used to produce extracellular proteases through submerged fermentation using cactus pear extract (Opuntia ficus-indica Mill.). A 2 3 factorial design was applied to optimize the protease production using three independent variables, namely temperature, pH and concentration of yeast extract, was also used a Central Composite Design (CCD) under Response Surface Methodology (RSM). All variables and interactions analyzed in the factorial design were significant or marginally significant, a Central Composite Design was developed, and the Response Surface Methodology towards the highest point it was established. The experimental model was validated under 14°C, pH 7.54, and 0.55% yeast extract, showing a protease activity of 447.65 7 2.6 U/mL by a prediction model of 445.48 U/mL. The enzyme showed a molecular weight of 59 kDa; it was inhibited in the presence of PMSF (serine protease); it presented optimal conditions at pH 8.0 and 50°C; it remained stable at pH in the 3.0-9.0 range and between 10 and 40°C; it showed a tolerance to 3000 mM NaCl as well as to surfactants, hydrogen peroxide and urea at 5%. This paper presents a proposal for an economically attractive production methodology using cactus pear as a primary source of carbon. In addition, the protease secreted by Acremonium sp. L1-4B presented a combination of biochemical characteristics that grants a promising variability of biotechnological applications.

show abstract

Medium optimization of protease production by Brevibacterium linens DSM 20158, using statistical approach

Cited by 21 publications

References 17 publications

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

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

Extracellular serine proteases by Acremonium sp. L1-4B isolated from Antarctica: Overproduction using cactus pear extract with response surface methodology

Contact Info

Product

Resources

About

Medium optimization of protease production by Brevibacterium linens DSM 20158, using statistical approach

Cited by 21 publications

References 17 publications

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

Enhanced production of chitin deacetylase by Penicillium oxalicum SAEM-51 through response surface optimization of fermentation conditions

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

Extracellular serine proteases by Acremonium sp. L1-4B isolated from Antarctica: Overproduction using cactus pear extract with response surface methodology

Contact Info

Product

Resources

About

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