Summary
Two β-(1→4)-endoglucanases have been purified from industrial waste broth of Aspergillus niger grown under conditions which produce citric acid. Molecular weights for endoglucanase A were 43,000 and 25,000 for endoglucanase B. Both enzymes exhibited very similar properties: a rather broad pH optimum between pH 2 and 7 for CM-cellulose hydrolysis and an inability to degrade crystalline cellulose. The endoglucanases have a higher thermal stability at acid pH (up to 60°C) than at alkaline pH. They are inhibited by iodine, HgCl2 and N-bromosuccinimide.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Clarke AE, Stone BA (1965a) Properties of a β-(1→4)-glucan hydrolase from Aspergillus niger. Biochem J 96:802–807
Clarke AE, Stone BA, (1965b) β-glucan hydrolases from Aspergillus niger. Biochem J 96:793–801
Davis BJ (1964) Disc electrophoresis. 2. Method and application to human serum protein. Ann N Y Acid Sci 121:404–427
Goksöyr J, Eriksen J (1980) Cellulases. In: Rose AH (ed) Microbial enzymes and bioconversions. Academic Press, London, pp 283–330
Hurst PL, Nielsen J, Sullivan PA, Shepherd MG (1977a) Purification and properties of a cellulase from Aspergillus niger. Biochem J 165:33–41
Hurst PL, Sullivan PA, Shepherd MG (177b) Chemical modification of a cellulase from Aspergillus niger. Biochem J 167:549–556
Hurst PL, Sullivan PA, Shepherd MG (1978) Substrate specificity and mode of action of a cellulase from Aspergillus niger. Biochem J 169:389–395
Ikeda R, Yamamoto T, Funatsu M (1967) Purification and some properties of cellulase from Aspergillus niger. Agr Biol Chem 31:1201–1209
Ikeda R, Yamamoto T, Funatsu M (1973a) Purification and some physical properties of acid cellulase from Aspergillus niger. Agr Biol Chem 37:1153–1159
Ikeda R, Yamamoto T, Funatsu M (1973b) Chemical and enzymatic properties of acid cellulase produced by Aspergillus niger. Agr Biol Chem 37:1169–1175
Janda W (1983) Fruit juice. In: Godfrey T, Reichelt J (eds) Industrial enzymology. Nature Press, New York, pp 315–320
Kosaric N, Wieszorek A, Cosentino GP, Magee RJ, Prenosil J (1983) Ethanol fermentation. In: Rehm HJ, Reed G (eds) Biotechnology, vol 3. Verlag Chemie, Weinheim, pp 257–385
Lowry H, Rosenbrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Peterson G (1963) Separation of cellulases on Sephadex G-100. Biochim Biophys Acta 77:665–667
Rauen HM (1956) Biochemisches Taschenbuch, Springer, Berlin, p 649
Röhr M, Kubicek CP, Kominek J (1983) Citric acid. In: Rehm HJ, Reed G (eds) Biotechnology, vol 3. Verlag Chemie, Weinheim, pp 419–454
Ryu DDY, Mandels M (1980) Cellulases: Biosynthesis and applications. Enzyme Microbiol Technol 2:91–102
Somogy M (1952) Notes on sugar determination. J Biol Chem 195:19–23
Suhar A, Maljevac I, Poljšak Z, Kotnik M, Derenčin M, Puidar V, Turk V (1982) Pectinases and proteinases from industrial waste broth of Aspergillus niger used to produce citric acid. In: Dupuy P (ed) Use of enzymes in food technology. Technique et documentation Lavoisier, Paris, pp 399–403
Tong CC, Cole AL, Shepherd MG (1980) Purification and properties of the cellulases from the thermophilic fungus Thermoascus aurantiacus. Biochem J 191:83–94
Whitaker JR (1963) Determination of molecular weight of proteins by gel filtration on Sephadex. Anal Chem 35:1950–1953
Wood TM, McCrae SI (1978) The cellulase of Trichoderma koningii. Biochem J 171:61–72
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Vidmar, S., Turk, V. & Kregar, I. Cellulolytic complex of Aspergillus niger under conditions for citric acid production. Isolation and characterization of two β-(1→4)-glucan hydrolases. Appl Microbiol Biotechnol 20, 326–330 (1984). https://doi.org/10.1007/BF00270594
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00270594