• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of biochemjBJ Latest papers and much more!
Biochem J. Feb 1, 1978; 169(2): 389–395.
PMCID: PMC1184178

Substrate specificity and mode of action of a cellulase from Aspergillus niger.


The mode of action and substrate specificity of a cellulase purified from Aspergillus niger were examined. The enzyme showed little capacity to hydrolyse highly ordered cellulose, but readily attacked soluble cellulose derivatives and amorphous alkali-swollen cellulose. Activity towards barley glucan and lichenin was greater than with CM-cellulose. Low activity was detected with CM-pachyman (a substituted beta-1,3-glucose polymer) and xylan. Activity towards yeast glucan, mannan, ethlene glycol chitin, glycol chitosan, laminarin, polygalacturonic acid and pectin could not be demonstrated. Cellobiose and p-nitrophenyl beta-D-glucoside were not hydrolysed, whereas the rate of hydrolysis of the higher members of the reduced cellulodextrins increased with chain length. The central bonds of cellotetraosylsorbitol and cellopentaosylsorbitol were the preferred points of clevage. Kinetic data indicated that the specificity region of the cellulase is five glucose units in length. The evidence indicates that the cellulase is an endoglucanase.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.0M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Abramowitz N, Schechter I, Berger A. On the size of the active site in proteases. II. Carboxypeptidase-A. Biochem Biophys Res Commun. 1967 Dec 29;29(6):862–867. [PubMed]
  • Berger A, Schechter I. Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):249–264. [PubMed]
  • Berghem LE, Pettersson LG, Axiö-Fredriksson UB. The mechanism of enzymatic cellulose degradation. Purification and some properties of two different 1,4beta-glucan glucanohydrolases from Trichoderma viride. Eur J Biochem. 1976 Jan 15;61(2):621–630. [PubMed]
  • Blake CC, Johnson LN, Mair GA, North AC, Phillips DC, Sarma VR. Crystallographic studies of the activity of hen egg-white lysozyme. Proc R Soc Lond B Biol Sci. 1967 Apr 18;167(1009):378–388. [PubMed]
  • Clarke AE, Stone BA. beta-glucan hydrolases from Aspergillus niger. Isolation of a beta-(1-4)-glucan hydrolase and some properties of the beta-(1-3)-glucan-hydrolase components. Biochem J. 1965 Sep;96(3):793–801. [PMC free article] [PubMed]
  • Clarke AE, Stone BA. Properties of a beta-(1-4)-glucan hydrolase from Aspergillus niger. Biochem J. 1965 Sep;96(3):802–807. [PMC free article] [PubMed]
  • Clarke AE, Stone BA. Enzymic hydrolysis of barley and other beta-glucans by a beta-(1--4)-glucan hydrolase. Biochem J. 1966 Jun;99(3):582–588. [PMC free article] [PubMed]
  • Eriksson KE, Hollmark BH. Kinetic studies of the action of cellulase upon sodium carboxymethyl cellulose. Arch Biochem Biophys. 1969 Sep;133(2):233–237. [PubMed]
  • HANSTEIN EG, WHITAKER DR. Improved procedures for preparation and characterization of myrothecium cellulase. 4. Characterization of activity toward beta-methyl glycosides of 1--4-beta-d-oligoglucosides. Can J Biochem Physiol. 1963 Mar;41:707–718. [PubMed]
  • HASH JH, KING KW. On the nature of the beta-glucosidases of Myrothecium verrucaria. J Biol Chem. 1958 May;232(1):381–393. [PubMed]
  • HOLDEN M. A study of enzymes that can break down tobacco-leaf components; unfractionated fungal enzymes. Biochem J. 1950 Oct;47(4):426–431. [PMC free article] [PubMed]
  • Hurst PL, Nielsen J, Sullivan PA, Shepherd MG. Purification and properties of a cellulase from Aspergillus niger. Biochem J. 1977 Jul 1;165(1):33–41. [PMC free article] [PubMed]
  • Kanda T, Wakabayashi K, Nisizawa K. Xylanase activity of an endo-cellulase of carboxymethyl-cellulase type from Irpex lacteus (Polyporus tulipiferae). J Biochem. 1976 May;79(5):989–995. [PubMed]
  • LI LH, KING KW. Fractionation of beta-glucosidases and related extracellular enzymes from Aspergillus niger. Appl Microbiol. 1963 Jul;11:320–325. [PMC free article] [PubMed]
  • Li LH, Flora RM, King KW. Individual roles of cellulase components derived from Trichoderma viride. Arch Biochem Biophys. 1965 Aug;111(2):439–447. [PubMed]
  • Pettersson G. Studies on cellulolytic enzymes. VI. Specificity and mode of action on different substrates of a cellulase from Penicillium notatum. Arch Biochem Biophys. 1969 Mar;130(1):286–294. [PubMed]
  • Phillips David C. THE HEN EGG-WHITE LYSOZYME MOLECULE. Proc Natl Acad Sci U S A. 1967 Mar;57(3):483–495. [PMC free article]
  • Shikata S, Nsizawa K. Purification and properties of an exo-cellulase component of novel type from Trichoderma miride. J Biochem. 1975 Sep;78(3):499–512. [PubMed]
  • Streamer M, Eriksson KE, Pettersson B. Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cullulose. Functional characterization of five endo-1,4-beta-glucanases and one exo-1,4-beta-glucanase. Eur J Biochem. 1975 Nov 15;59(2):607–613. [PubMed]
  • SVENNERHOLM L. The quantitative estimation of cerebrosides in nervous tissue. J Neurochem. 1956 May;1(1):42–53. [PubMed]
  • WHITAKER DR. Hydrolysis of a series of beta-1,4'-oligoglucosides by Myrothecium verrucaria cellulase. Arch Biochem Biophys. 1954 Dec;53(2):439–449. [PubMed]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...