Phytase production by the thermophilic fungus Rhizomucor pusillus

Chadha, Bhupinder Singh; Harmeet, Gulati; Mandeep, Minhas; Saini, Harvinder Singh; Singh, Nand Kumar

doi:10.1023/b:wibi.0000013319.13348.0a

Cited by 93 publications

(70 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The optimization of phytase production was carried out by Box-Behnken design of experiments resulting in the maximum level of phytase production i.e. 9.18 U/g of substrate [32]. All these findings using statistical optimization are in close agreement with our results.…”

Section: Discussionsupporting

confidence: 85%

Optimization of media components for laccase production by litter dwelling fungal isolate Fusarium incarnatum LD‐3

Chhaya

Gupte

2010

J. Basic Microbiol.

View full text Add to dashboard Cite

Laccase production by solid state fermentation (SSF) using an indigenously isolated litter dwelling fungus Fusarium incarnatum LD-3 was optimized. Fourteen medium components were screened by the initial screening method of Plackett-Burman. Each of the components was screened on the basis of 'p' (probability value) which was above 95% confidence level. Ortho-dianisidine, thiamine HCl and CuSO(4) . 5 H(2)O were identified as significant components for laccase production. The Central Composite Design response surface methodology was then applied to further optimize the laccase production. The optimal concentration of these three medium components for higher laccase production were (g/l): CuSO(4) . 5 H(2)O, 0.01; thiamine HCl, 0.0136 and ortho-dianisidine, 0.388 mM served as an inducer. Wheat straw, 5.0 g was used as a solid substrate. Using this statistical optimization method the laccase production was found to increase from 40 U/g to 650 U/g of wheat straw, which was sixteen times higher than non optimized medium. This is the first report on statistical optimization of laccase production from Fusarium incarnatum LD-3.

show abstract

Section: Discussionsupporting

confidence: 85%

Optimization of media components for laccase production by litter dwelling fungal isolate Fusarium incarnatum LD‐3

Chhaya

Gupte

2010

J. Basic Microbiol.

View full text Add to dashboard Cite

show abstract

“…The reaction was stopped by adding an equal volume (200 l) of 15% trichloroacetic acid after 30 min of incubation at 50°C [3]. The liberated phosphate ions were quantiWed by mixing 100 l of assay mixture with 900 l of developing reagent containing 0.76 M H 2 SO 4 -2.5% ascorbic acid-0.06% ammonium molybdate (3:1:0.1).…”

Section: Enzyme Assaymentioning

confidence: 99%

Production and characterization of thermostable alkaline phytase from Bacillus laevolacticus isolated from rhizosphere soil

Gulati

Chadha

Saini

2006

J Ind Microbiol Biotechnol

107

View full text Add to dashboard Cite

Proteases are one of the largest groups of hydrolytic enzymes constituting about 60% of total worldwide sales of industrial enzymes due to their wide applications in detergent, leather, textile, food and pharmaceutical industry. Microbial proteases have been preferred over animal and plant proteases because of their fundamental features and ease in production. Bacillus infantis SKS1, an alkaline protease producing bacteria has been isolated from garden soil of north India and identified using morphological, biochemical and molecular methods. 16S rDNA sequence amplified using universal primers has 99% sequence identity with corresponding gene sequence of Bacillus infantis strain FM 34 and Bacillus sp. Beige. The bacterial culture and its 16S rDNA gene sequence have been deposited to Microbial Culture Collection (Pune, India) with accession number MCC 3035 and GenBank with accession number KR092197 respectively. The partially purified extract of Bacillus infantis SKS1 was thermostable and active in presence of Mg 2+ , acetyl acetone and laundry detergents implicating its application in industry. Production of these enzymes using this strain was maximized by optimization of various parameters including temperature, pH, media components and other growth conditions. Our results show that fructose and dextrose serve as the best carbon sources for production of these enzymes, highlighting the use of this strain for enzyme production utilizing relatively inexpensive substrates like beet molasses and corn steep liquor. Additionally, this strain showed maximum production of enzymes at 40˚C similar to bacterial species used for commercial production of alkaline proteases. Characterization of alkaline proteases from this strain of Bacillus infantis and optimization of parameters for its production would help in understanding its industrial application and large-scale production.

show abstract

“…Many phytases from other microorganisms showed much higher thermostability, but were poorly active at 37°C (Wyss et al 1998;Vohra and Satyanarayana 2001), making them unsuitable as animal-feed additives. Therefore, it is necessary to utilize new phytase resources and obtain better phytases (Tseng et al 2000;Miksch et al 2002;Chadha et al 2004;Cho et al 2005;Guo et al 2007;Nakashima et al 2007;Huang et al 2008;Pavlova et al 2008;Shi et al 2008;Zhang and Lei 2008).…”

Section: Introductionmentioning

confidence: 99%

A novel thermostable phytase from the fungus Aspergillus aculeatus RCEF 4894: gene cloning and expression in Pichia pastoris

Jiang

et al. 2010

World J Microbiol Biotechnol

View full text Add to dashboard Cite

A novel gene of thermostable phytase, phyA, was isolated by polymerase chain reaction (PCR) techniques from Aspergillus aculeatus RCEF 4894. The fulllength phyA gene comprises 1,404 bp and encodes 467 amino-acid residues, including a 19-residue putative N-terminal signal peptide. The phytase of A. aculeatus was a novel addition to the histidine-acid phosphatase family, as evidenced by both the conserved motifs RHGXRXP and HD in the amino-acid sequence, and 3D structure models. The recombinant phytase was overexpressed in Pichia pastoris, and its specific activity reached 3,000 U mL -1 at the optimum pH of 5.5. This recombinant, thermostable phytase was able to withstand temperatures of up to 90°C for 10 min, with a loss of only 13.9% of initial enzymatic activity, and showed high activity with phytic-acid sodium salt at a pH range of 2.5-6.5. The broad pH optima and high thermostability of the phytase makes it a promising candidate for feed-pelleting applications.

show abstract

Phytase production by the thermophilic fungus Rhizomucor pusillus

Cited by 93 publications

References 18 publications

Optimization of media components for laccase production by litter dwelling fungal isolate Fusarium incarnatum LD‐3

Optimization of media components for laccase production by litter dwelling fungal isolate Fusarium incarnatum LD‐3

Production and characterization of thermostable alkaline phytase from Bacillus laevolacticus isolated from rhizosphere soil

A novel thermostable phytase from the fungus Aspergillus aculeatus RCEF 4894: gene cloning and expression in Pichia pastoris

Contact Info

Product

Resources

About