Molecular characterization of multiple xylanase producing thermophilic/thermotolerant fungi isolated from composting materials

Sharma, Manju; Chadha, Bhupinder Singh; Kaur, Manpreet; Ghatora, Sonia; Saini, Harvinder Singh

doi:10.1111/j.1472-765x.2008.02357.x

Cited by 58 publications

(34 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The DNA was precipitated with 9 parts of ice cold isopropyl alcohol and 1 part of sodium acetate (3 mol l -1 ; pH 8.0) and kept at -20°C for 2 h, followed by centrifugation for 15 min at 8,000g. The DNA pellet was rinsed with 70% (v/v) ethanol, air dried, suspended in 50 ll of sterilized double distilled water and stored at 4°C (Sharma et al 2008).…”

Section: Isolation Of Dnamentioning

confidence: 99%

Molecular and functional characterization of endophytic fungi from traditional medicinal plants

Bhagat

Kaur

Sharma

et al. 2011

World J Microbiol Biotechnol

View full text Add to dashboard Cite

This study reports the isolation of 63 endophytic fungal isolates from two traditional medicinal plants, Ocimum sanctum and Sapindus detergens from different locations of Amritsar, India. The functional characterization of the fungi for their ability to produce anti bacterial and anti cancer agent was carried out. Sixteen strains were characterized at molecular level by sequencing the amplified ITSI-5.8-ITSII region of rDNA. The phylogenetic tree resolved the endophytic fungi into different clades. The fungal endophytes belonging to order Pleosporales (Alternaria sp., Phoma sojicola and Exserohilum sp.) were functionally versatile as they produced diverse biomolecules including antibacterial agent active against Mycobacterium smegmatis, as well as cytotoxic activity against different human cancer cell lines of lung, ovary, breast, prostrate, neuroblastoma and colon.

show abstract

Section: Isolation Of Dnamentioning

confidence: 99%

Molecular and functional characterization of endophytic fungi from traditional medicinal plants

Bhagat

Kaur

Sharma

et al. 2011

World J Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…A thermotolerant fungal strain isolated from compositing soil was identified as Aspergillus nidulans on the basis of morphology and molecular characterization based on sequencing of ITSI-5.8S-ITSII amplified rDNA [11]. The fungus was grown and maintained on YpSs medium of the following composition (% w/v), starch 1.5; yeast extract 0.4; KH 2 PO 4 0.2 K 2 HPO 4 0.23; MgSO4 0.05; Citric acid 0.057 and agar 2.0.…”

Section: Culturementioning

confidence: 99%

Comparative analysis of two catalytically distinct endoglucanases from Aspergillus nidulans

Kaur¹,

Chadha²,

Oberoi³

2015

J App Biol Biotech

View full text Add to dashboard Cite

This study reports purification and characterization of two catalytically distinct endoglucanases (EGI and EGII) from a thermotolerant fungus Aspergillus nidulans. The endoglucanases (EGI and EGII) exhibited molecular masses of 56 and 31 kDa and pIs of 3.6 and 3.8, respectively. EGI was putatively classified as GH7 family member catalyzed carboxymethyl cellulose, xyloglucan, barley β-glucan as well as pNP-β-D-lactopyranoside and pNP-cellobioside, and was optimally active at 50°C and pH 4.0. Whereas, EGII lacking CBD preferentially recognized barley β-glucan when compared substrate CMC, xyloglucan and lichenan and was putatively classified as GH12 member. Interestingly, EGII was characterized to be thermoacidophilic exhibiting 96% its activity at pH 2.0 and at 60 °C. Hydrolysis of barley β-glucan and CMC by EGI and EGII liberated cellobiose as a major product. HPLC analysis showed that barley β-glucan hydrolysate obtained by action of EGI showed high levels of glucose in addition to cellobiose indicating towards an exo type action of this enzyme. Key words:Thermoacidophilic endoglucanases, GH7, GH12, barley β-glucan 1.INTRODUCTIONCellulose has a great potential as a renewable energy source and has gained interest of biotechnology community on their exploration for biofuel production and other value added products. Cellulose is a linear homo-polymer of D-glucose monomers linked together through β-1-4 glycosidic bonds and mainly forms the structural cell wall component in both the lower and higher plants [1]. The biodegradation of complex polymeric structure of cellulose is primarily attributed to multi-component enzyme system that works in a synergistic manner. These enzymes are comprises of endoglucanase (EC 3.2.1.74), which attack cellulose in amorphous zone and release oligomers, cellobiohydrolases (CBHI & CBHII) (EC 3.2.1.91), that liberate cellobiose from reducing and non-reducing ends, and β-glucosidase (EC 3.2.1.21), which hydrolyze cellobiose to glucose [2]. Endoglucanases are widely classified on the basis of different characteristics into families GH 5,6,7,8,9,12, 45 & 74 [3]. Due to intensive research on the structural, catalytic and functional roles, both bacterial and fungal cellulases have led their use in various fields [4]; [5]. In addition to their potential use in the biofuel industry, for degradation of agro-residual waste into simple sugars which can be further fermented, cellulases are widely employed in increasing the yield of fruit juices, beer filtration, paper and pulp industry as well as improving animal feed stock [6]; [7]. With increasing demand for endoglucanases, . * Corresponding Author E-mail: baljit_sohal@rediffmail.comidentification of new EGs, especially thermoacidophilic, with good properties for improved performance is highly desirable [8]. Different endoglucanases from the same family show difference in their substrate specificity as well as different optimum pH and temperature and therefore needs to be characterized [9]. In the present study, we have reported the comparative...

show abstract

“…A variety of xylanases have been reported from fungi, bacteria, and yeast, and some of the corresponding genes have been cloned and expressed [2][3][4]. Based on the primary structure of the catalytic domain, most xylanases are confined to glycoside hydrolase (GH) families 10 and 11 [5].…”

Section: Introductionmentioning

confidence: 99%

A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability

Bai

Wang

Zhang

et al. 2009

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

We have identified a highly pH-adaptable and stable xylanase (XynA4) from the thermoacidophilic Alicyclobacillus sp. A4, a strain that was isolated from a hot spring in Yunnan Province, China. The gene (xynA4) that encodes this xylanase was cloned, sequenced, and expressed in Escherichia coli. It encodes a 338-residue polypeptide with a calculated molecular mass of 42.5 kDa. The deduced amino acid sequence is most similar to (53% identity) an endo-1,4-beta-xylanase from Geobacillus stearothermophilus that belongs to family 10 of the glycoside hydrolases. Purified recombinant XynA4 exhibited maximum activity at 55 degrees C and pH 7.0, had broad pH adaptability (>40% activity at pH 3.8-9.4) and stability (retaining >80% activity after incubation at pH 2.6-12.0 for 1 h at 37 degrees C), and was highly thermostable (retaining >90% activity after incubation at 60 degrees C for 1 h at pH 7.0). These properties make XynA4 promising for application in the paper industry. This is the first report that describes cloning and expression of a xylanase gene from the genus Alicyclobacillus.

show abstract

Molecular characterization of multiple xylanase producing thermophilic/thermotolerant fungi isolated from composting materials

Cited by 58 publications

References 31 publications

Molecular and functional characterization of endophytic fungi from traditional medicinal plants

Molecular and functional characterization of endophytic fungi from traditional medicinal plants

Comparative analysis of two catalytically distinct endoglucanases from Aspergillus nidulans

A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability

Contact Info

Product

Resources

About