Abstract
The continuous exploration of new microbial cell factories in diverse environmental and geographical locations has led to pivotal developments in the production of industrially important extracellular metabolites. Filamentous fungi are used for large-scale production of various enzymes, and amylolytic enzymes in particular. Among them, amyloglucosidase is known to be secreted extracellularly in copious amounts. The current investigation was based on molecular phylogeny and taxonomy of filamentous fungi from the genus Aspergillus that are capable of producing amyloglucosidase under submerged fermentation conditions. Optimization of physical and chemical cultivation parameters were also investigated. Among the various natural isolates identified in the current study, Aspergillus fumigatus KIBGE-IB33 was selected based on maximum enzyme production. Parametric optimization resulted in the secretion of maximum amyloglucosidase in a modified starch medium. High enzyme yield was achieved after 4 days of fermentation at 30 °C in a starch-based medium (pH 7.0). The mesophilic nature of this isolate, with its broad pH range and reduced fermentation time, renders A. fumigatus KIBGE-IB33 an attractive candidate for large-scale production of amyloglucosidase for starch saccharification.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Aguilar G, Morlon-Guyot J, Trejo-Aguilar B, Guyot JP (2000) Purification and characterization of an extracellular alpha amylase produced by Lactobacillus manihotivorans LMG 1801 (T), an amylolytique lactic acid bacterium. Enzyme Microb Technol 27:406–413
Babu KR, Satyanarayana T (1993) Extracellular calcium inhibited α-amylase of Bacillus coagulans B49. Enzyme Microb Technol 15:1066–1069
Djekrif-Dakhmouche S, Gheribi-Aoulmi Z, Meraihi Z, Bennamoun L (2006) Application of statistical design to the optimization of culture medium for α-amylase production by Aspergillus niger ATCC 16404 grown on orange waste powder. J Food Eng 73:190–197
Fogarty WM, Kelly CT (1990) Recent advances in microbial amylases. In: Fogarty WM, Kelly CT (eds), Microbial enzymes and biotechnology. 2nd edn. Elsevier, Applied Science Publishers
Ghani M, Aman A, Rehman H, Siddiqui NN, Qader SA (2013) Strain improvement by mutation for enhanced production of starch-saccharifying glucoamylase from Bacillus licheniformis. Starch/Stärch 65:875–884
Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B (2003) Microbial α-amylase: A biotechnological perspective. Process Biochem 38:1599–1616
Karthikeyan V, Patharajan S, Polani P, Spadaro D, Gullino ML, Garibaldi A (2010) Modified simple protocol for efficient fungal DNA extraction highly suitable for PCR base molecular methods. Global Journal of Molecular Sciences 5:37–42
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–375
McTigue MA, Kelly CT, Fogarty WM, Doyle EM (1994) Production studies on the alkaline amylase of three alkalophilic Bacillus spp. Biotechnol Lett 16:569–574
Mertens JA, Skory CD (2007) Isolation and characterization of two genes that encode active glucoamylase without a starch binding domain from Rhizopus oryzae. Curr Microbiol 54:462–466
Michelin M, Ruler R, Ward RJ, Moraes LAB, Jorge JA, Terenzi HF, Polozeli MLTM (2008) Purification and biochemical characterization of a thermostable extracellular glucoamylase produced by the thermotoleratnt fungus Paecilomyces variotii. J Ind Microbiol Biotechnol 35:17–25
Norouzian D, Akbarzadeh A, Scharer JM, Young MM (2006) Fungal glucoamylase. Biotechnol Adv 24:80–85
Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R (2000) Advances in microbial amylases. Biotechnol Appl Biochem 1543:135–152
Patil SR, Dayanand A (2005) Optimization of process for the production of fungal pectinase from deseeded sunflower head in submerged and solid-state conditions. Bioresour Technol 97:2340–2344
Santamaria RI, Del-Rio G, Saab G, Rodriguez ME, Soberon X, Lopez-Marguia A (1999) Alcoholysis reactions from starch with α-amylases. FEBS Letters 452:346–350
Shaku M, Koike S, Udaka S (1980) Culture condition for protein production by Bacillus brevis No. 47. Agr Biol Chem 44:99–103
St-Germain G, Summerbell R (1996) Identifying filamentous fungi - A Clinical Laboratory Handbook. 1st edn. Belmont, Star Publishing Company, California. Publishers, London, pp 71–132
Trinder P (1969a) Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor. Ann Clin Biochem 6:24–28
Trinder P (1969b) Determination of glucose in blood using 4-amino phenazone as oxygen acceptor. J Clin Pathol 22:246
Yoon MY, Yoo YJ, Cadman TW (1989) Phosphate effect in the fermentation of α-amylase by Bacillus amyloliquefaciens. Biotechnol Lett 11:59–60
Zambare V (2010) Solid state fermentation of Aspergillus oryzae for glucoamylase production on agro residues. International Journal of Life Sciences 4:16–25
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Pervez, S., Siddiqui, N.N., Ansari, A. et al. Phenotypic and molecular characterization of Aspergillus species for the production of starch-saccharifying amyloglucosidase. Ann Microbiol 65, 2287–2291 (2015). https://doi.org/10.1007/s13213-015-1070-9
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13213-015-1070-9