Characterization of the purified multifunctional cellulase component of Penicillium funiculosum

Sahasrabudhe, N.A.; Lachke, Anil; Ranjekar, P. K.

doi:10.1007/bf01026203

Cited by 11 publications

(4 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition to the complexity of the multi-enzymatic system, the variability of the enzymatic assays reported in literature made it difficult to compare the K mapp values of cellulases from different sources. Nevertheless, the K mapp (Table 1) of the endo-1,4-β-D-glucanase (3.55 mg mL -1 ) was lower than that reported (33) for the same enzyme from another P. funiculosum strain (20 mg mL -1 ); however, close K mapp values (2.0-4.8 mg mL -1 ) have been reported (27) for two isoenzymes of endo-1,4-β-Dglucanase from P. pinophilum. On the other hand, the K mapp of cellobiohydrolase (2.59 mM) was higher than that reported for the same enzyme from another P. funiculosum strain (0.85 mM), using cello-oligosaccharide as substrate (6).…”

Section: Resultscontrasting

confidence: 66%

Characterization of Selected Cellulolytic Activities of Multi-enzymatic Complex System from Penicillium funiculosum

Karboune¹,

Geraert²,

Kermasha³

2008

J. Agric. Food Chem.

View full text Add to dashboard Cite

The presence of endo-1,4-beta-D-glucanase, cellobiohydrolase, and beta-glucosidase activities in a multi-enzymatic complex system from Penicillium funiculosum was investigated. The interesting feature of these enzymes is their synergistic action for the hydrolysis of the native cellulose into glucose units. Both endo-1,4-beta-D-glucanase and cellobiohydrolase showed broader pH activity profiles, with pH optima of 4.0 and 4.0-5.0, respectively. However, beta-glucosidase activity showed a narrow pH-activity profile, with an optimum pH of 4.5. The different cellulolytic activities were stable in the acidic pH range of 2.5-6.0 and showed a similar optimal temperature of 60 degrees C. Although beta-glucosidase has shown a close catalytic efficiency as that of endo-1,4-beta-D-glucanase, its thermal stability was lower. However, the thermal stability profile of cellobiohydrolase was close to that of endo-1,4-beta-D-glucanase. The results also revealed the presence of high levels of endo-1,3-1,4-beta-D-glucanase, endo-1,3-beta- d-glucanase, and pectinase activities in the multi-enzymatic cellulolytic complex system. Moreover, the investigated multi-enzymatic complex system was effective in degrading the nonstarch polysaccharides of soybean meal.

show abstract

Section: Resultscontrasting

confidence: 66%

Characterization of Selected Cellulolytic Activities of Multi-enzymatic Complex System from Penicillium funiculosum

Karboune¹,

Geraert²,

Kermasha³

2008

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…The overall results indicate that the endo-1,3-1,4--D-glucanase specific activity exhibited higher thermal stability than that of endo-1,4--D-xylanase. Similarly, Sahasrabudhe et al 35) have reported that the thermal stability of endoglucanase from P. funiculosum was greater than that of the endo-1,4--D-xylanase. The experimental findings (Fig.…”

Section: )mentioning

confidence: 99%

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Karboune¹,

L’Hocine²,

Anthoni³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

A multi-enzymatic system from Penicillium funiculosum displayed -L-arabinofuranosidase, endo-1,4--Dxylanase, -D-xylosidase and endo-1,3-1,4--D-glucanase activities at high levels over a wide acidic pH range of 2.0 to 5.5. Moreover, the pH stability was particularly extended over the wide range of pH of 2.0 to 8.0 with endo-1,3-1,4--D-glucanase and endo-1,4--D-xylanase; however, -L-arabinofuranosidase and -D-xylosidase exhibited higher stability in the pH range of 2.0 to 5.5. The results indicate that the optimal temperature of -L-arabinofuranosidase (65 C) and -D-xylosidase (70 C) as well as their thermal stability were higher than those of endo-1,3-1,4--D-glucanase (60 C) and endo-1,4--D-xylanase (50 C). Although V maxapp of -Dxylosidase and endo-1,4--D-xylanase was higher than that of -L-arabinofuranosidase and endo-1,3-1,4--Dglucanase, respectively, their catalytic efficiency was lower. High levels of ferulolyl esterase, -D-galactosidase, -D-mannosidase and endo-1,4--D-mannanase activities were also detected in the multi-enzymatic system. The overall features of the multi-enzymatic system from P. funiculosum reveal its potential for degrading and modifying plant cell walls from a variety of food and feedstuffs.

show abstract

“…The CBH belongs to three different glycoside hydrolase families namely GH6, GH7 and GH48. The importance of two cellobiohydrolases, CBH1 and CBHII has been realized for their preferences to act on the reducing and nonreducing ends of cellulose chains of microcrystalline cellulose [14,29,32] In fungi, the presence of CBH1 is needed for ordered degradation of cellulose, which requires all three structural modules of the cellulase i.e., the CD, C-terminal CBD, and linker region [33]. The fungus Penicillium funiculosum is a filamentous fungus an efficient producer of cellulase [34] [27].…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Expression of a Family 7 Cellobiohydrolase Gene Cbh1 From Penicillium Funiculosum Ncl1

Vanitha¹,

Meera²,

Ramani³

et al. 2011

Int J of Micr Res

View full text Add to dashboard Cite

A cellobiohydrolase gene cbh1 was cloned from a cellulolytic fungus, Penicillum funiculosum NCL1. Nucleotide sequencing of cbh1 gene revealed that this gene was 1590 bp length encoding a putative protein consisting of 529 amino acids. The deduced amino acid sequence showed that the predicted molecular mass of the CBHI was 54.9 kDa, and showed significant homology to glycoside hydrolase family 7 cellobiohydrolases. The cbh1 gene was cloned using pET30b and expressed in E. coli BL21 (DE3). The expression analysis of the recombinant E. coli BL21 (pETC7) revealed the production of cbh1 transcript; however, functional cellobiohydrolase could not be detected. Therefore, the cbh1 gene was sub-cloned into GST tagged expression vector pGEX4t-3. The GST tagged cellobiohydrolase was purified to homogeneity using affinity chromatography. The recombinant enzyme exhibited optimum catalytic activity at pH 5.0 and 50 °C respectively. It was thermostable at 50 °C and retained 70% of its original activity after 30 min at 60 °C.

show abstract

Characterization of the purified multifunctional cellulase component of Penicillium funiculosum

Cited by 11 publications

References 14 publications

Characterization of Selected Cellulolytic Activities of Multi-enzymatic Complex System from Penicillium funiculosum

Characterization of Selected Cellulolytic Activities of Multi-enzymatic Complex System from Penicillium funiculosum

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Molecular Cloning and Expression of a Family 7 Cellobiohydrolase Gene Cbh1 From Penicillium Funiculosum Ncl1

Contact Info

Product

Resources

About