Abstract
α-Amylase activities of Aspergillus oryzae grown on dextrin or indigestible dextrin were 7·8 and 27·7 U ml−1, respectively. Glucoamylase activities of the cultures grown on dextrin or indigestible dextrin were 5·4 and 301 mU ml−1, respectively. The specific glucoamylase production rate in indigestible dextrin batch culture reached 1·35 U g DW−1 h−1. In contrast, biomass concentration of A. oryzae in indigestible dextrin culture was 35% of that in dextrin culture. Thus, the culture method using indigestible dextrin has the potential to improve amylolytic enzyme production and fungal fermentation broth rheology.
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References
Agger T, Spohr AB, Nielsen J (2001) α-Amylase production in high cell density submerged cultivation of Aspergillus oryzae and A. nidulans. Appl Microbiol Biotechnol 1:81–84
Agger T, Petersen JB, O’Connor SM, Murphy RL, Kelly JM, Nielsen J (2002) Physiological characterisation of recombinant Aspergillus nidulans strains with different creA genotypes expressing A. oryzae alpha-amylase. J Biotechnol 3:279–285
Barbesgard P, Heldt-Hansen HP, Didenrichsen B (1992) On the safety of Aspergillus oryzae; a review. Appl Microbiol Biotechnol 36:569–572
Garcia-Ochota F, Gomez E (2009) Bioreactor scale-up and oxygen transfer rate in microbial process: an overview. Biotechnol Adv 27:153–176
Gomi K, Akeno T, Minetoki T, Ozeki K, Kumagai C, Okazaki N, Iimura Y (2000) Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae. Biosci Biotechnol Biochem 4:816–827
Imai Y, Suzuki M, Masamoto M, Nagayasu K, Kishimoto M (1994) Glucoamylase production of Aspergillus oryzae in fed-batch culture using a stastical regression model. J Ferment Bioeng 78:310–314
Kato N, Murakoshi Y, Kato M, Kobayashi T, Tsukagoshi N (2002) Isomaltose formed by alpha-glucosidases triggers amylase induction in Aspergillus nidulans. Curr Genet 1:43–50
Li ZJ, Shukala V, Fordyce AP, Pedersen AG, Wenger KS, Marten MR (2000) Fungal morphology and fragmentation behavior in a fed-batch Aspergillus oryzae fermentation at the production scale. Biotechnol Bioeng 70:300–312
Minetoki T, Gomi K, Kitamoto K, Kumagai C, Tamura G (1995) Characteristic expression of three amylase-encoding genes, agdA, amyB, and glaA in Aspergillus oryzae transformants containing multiple copies of the agdA gene. Biosci Biotechnol Biochem 12:2251–2254
Nakajima K, Asakura T, Maruyama J, Morita Y, Oike H, Shimizu-Ibuka A, Misaka T, Sorimachi H, Arai S, Kitamoto K, Abe K (2006) Extracellular production of neoculin, a sweet-tasting heterodimeric protein with taste-modifying activity by Aspergillus oryzae. Appl Environ Microbiol 5:3716–3723
Ohkuma K, Wakabayashi S (2001) Fibersol-2: a soluble, non-digestible, starch-derived dietary fibre. In: McCleary BV, Prosky L (eds) Advanced dietary fibre technology. Blackwell Science, Oxford, pp 509–552
Ohkuma K, Matsuda I, Katta Y, Hanno Y (1990) Pyrolysis of starch and its digestibility by enzyme. Denpun Kagaku 37:104–114 (in Japanese)
Petersen KL, Lehmbeck J, Christensen T (1999) A new transcriptional activator for amylase genes in Aspergillus. Mol Gen Genet 4–5:668–676
Ruijter GJ, Visser J (1997) Carbon repression in Aspergilli. FEMS Microbiol Lett 2:103–114
Sugimoto T, Horaguchi K, Shoji H (2011) Indigestible dextrin stimulates glucoamylase production in submerged culture of Aspergillus kawachii. J Ind Microb Biotechnol. doi:10.1007/s10295-011-0988-6
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The authors are thankful to Matsutani Chemical Industry, Japan, for the gift of indigestible dextrin.
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Sugimoto, T., Shoji, H. Indigestible dextrin is an excellent inducer for α-amylase, α-glucosidase and glucoamylase production in a submerged culture of Aspergillus oryzae . Biotechnol Lett 34, 347–351 (2012). https://doi.org/10.1007/s10529-011-0777-3
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DOI: https://doi.org/10.1007/s10529-011-0777-3