Cellulolytic Enzyme System of
            <i>Thermoactinomyces</i>
            sp. Grown on Microcrystalline Cellulose

Hagerdal, Bärbel; Ferchak, John D.; Pye, Erica

doi:10.1128/aem.36.4.606-612.1978

Cited by 106 publications

(18 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Separation of endoglucanase and exoglucanase activity in culture filtrates of Thin. curvata has been described [64,71] and Hfigerdal and coworkers [72] identified at least three extracellular cellulases in Thm. fusca.…”

Section: Actinomycete Cellulasesmentioning

confidence: 99%

“…Optimisation of cellulase production is usually achieved by empirical manipulation of growth conditions and is often species-or strain-specific. Actinomycete cellulases are produced and released into the medium during exponential growth, while /?-glucosidase activity remains associated with culture solids throughout [43, 44,72]. Cellulose degradation or cellulase production by cultures can be improved by altering the cellulose source and nitrogen source supplied [81,83,92,93].…”

Section: Actinomycete Cellulasesmentioning

confidence: 99%

See 1 more Smart Citation

Lignocellulose-degrading actinomycetes

McCarthy

1987

FEMS Microbiology Letters

View full text Add to dashboard Cite

Section: Actinomycete Cellulasesmentioning

confidence: 99%

Section: Actinomycete Cellulasesmentioning

confidence: 99%

Lignocellulose-degrading actinomycetes

McCarthy

1987

FEMS Microbiology Letters

View full text Add to dashboard Cite

“…Some bacteria and actinomycetes, such as Clostridium thermocellum, Ruminococcus albus, Acinetobacter anitratus, Branhamella sp., Streptomyces sp., Thermoactinomyces sp. and Thermomonospora curvata, have also been reported to yield cellulase activity (HÌgerdal, Ferchak & Pye 1978;Wood,Wilson & Stewart 1982;Nochur, Roberts & Demain 1993;Li & Gao 1996;Ekperigin 2007;Alani, Anderson & Moo-Young 2008). The species A. veronii isolated from an abalone has also been proven to be able to produce cellulase (Han & Cai 2005).…”

Section: Resultsmentioning

confidence: 99%

Cellulase-producing bacteria of Aeromonas are dominant and indigenous in the gut of Ctenopharyngodon idellus (Valenciennes)

Jiang

Xie

Yang

et al. 2011

Aquaculture Research

View full text Add to dashboard Cite

Herbivorous grass carp (Ctenopharyngodon idella) has a powerful capability to digest aquatic weed. Cellulase activity or cellulase-producing bacteria were found in the gut of grass carp. However, it remains uncertain whether the cellulase-producing bacteria were a part of indigenous intestinal microbiota that the ¢sh harboured or were introduced with food. In the present study, the bacterial diversities and population abundance in the gut of starved grass carps have been investigated by sequencing 16S rRNA gene libraries. The16S rRNA gene libraries revealed that 28 parasitic bacteria from gut were a⁄liated to seven genera of Vibrio, Acinetobacter, Providencia, Yersinia, Pseudominas, Morganella or Aeromonas, respectively, and Aeromonas was identi¢ed as the most dominant genus in the gut of C. idella. All of cellulase-producing bacteria isolated from the gut of C. idella in this research belonged to Aeromonas. On the whole, the results in this research showed that cellulase activity within C. idella should be at least partially resulting from bacteria of Aeromonas with cellulase-producing capabilities, which were indigenous and dominant intestinal species.

show abstract

“…However, lignocellulose degradation in natural substrates is largely attributed to fungi and, in this respect, the importance of actinomycetes may have been underestimated. Thus far, the best-characterized cellulase systems are those of Thermomonospora curvata and Thermomonospora fusca (Hagerdal et al 1978 ;Fennington et al 1983 ;Calza et al 1985). Although species of Streptomyces, an actinomycetes genus, appeared in the early studies on cellulolytic microorganisms (Enger and Sleeper 1965), their lignocellulase systems only recently have received much attention (Crawford 1978 ;Kluepfel et al 1986 ;Spear et al 1993).…”

Section: Introductionmentioning

confidence: 99%

Isolation and partial characterization of cellulose-degrading strain of Streptomyces sp. LX from soil

Gao

1996

Lett Appl Microbiol

View full text Add to dashboard Cite

A previous report dealt with the cloning in Escherichia coli and sequencing of both the cDNA and genomic DNA encoding a highly active xylanase (XynA) of Aureobasidium pullulans (X.-L. Li and L. G. Ljungdahl, Appl. Environ. Microbiol. 60:3160-3166, 1994). Now we show that the gene was expressed in Saccharomyces cerevisiae under the GAL1 promoter in pYES2 and that its product was secreted into the culture medium. S. cerevisiae clone pCE4 with the whole open reading frame of xynA, including the part coding for the signal peptide, had xylanase activity levels of 6.7 U ml-1 in the cell-associated fraction and 26.2 U ml-1 in the culture medium 4 h after galactose induction. Two protein bands with sizes of 25 and 27 kDa and N-terminal amino acid sequences identical to that of APX-II accounted for 82% of the total proteins in the culture medium of pCE4. These proteins were recognized by anti-APX-II antibody. The results suggest that the XynA signal peptide supported the posttranslational processing of xynA product and the efficient secretion of the active xylanase from S. cerevisiae. Clones pCE3 and pGE3 with inserts of cDNA and genomic DNA, respectively, containing only the mature enzyme region attached by a Met codon had low levels of xylanase activity in the cell-associated fractions (1.6 U ml-1) but no activity in the culture media. No xylanase activity was detected in clone pGE4, which was the same as pCE4, except that pGE4 had a 59-bp intron in the signal peptide region. A comparison of the A. pullulans and S. cerevisiae signal peptides demonstrated that the XynA signal peptide was at least three times more efficient than those of S. cerevisiae invertase or mating alpha-factor pheromone in secreting the heterologous xylanase from S. cerevisiae cells.

show abstract

Cellulolytic Enzyme System of Thermoactinomyces sp. Grown on Microcrystalline Cellulose

Cited by 106 publications

References 15 publications

Lignocellulose-degrading actinomycetes

Lignocellulose-degrading actinomycetes

Cellulase-producing bacteria of Aeromonas are dominant and indigenous in the gut of Ctenopharyngodon idellus (Valenciennes)

Isolation and partial characterization of cellulose-degrading strain of Streptomyces sp. LX from soil

Contact Info

Product

Resources

About