Abstract
In this paper, maltotriose was prepared by hydrolyzing of pullulan with pullulanase. The optimal hydrolyzing conditions were investigated and the optimum conditions were as follows: time 6 h; pH 5.0; temperature 45 °C; amount of pullulanase, 10 ASPU/g; concentration of pullulan, 3% (w/v). Under these conditions, the dextrose equivalent value reached up to 30.1. The hydrolysate was filtrated through a filter membrane that could intercept any particle whose molecular weight was more than 1,000 Da, concentrated to 20% (w/v) and precipitated with 8 volumes of ethanol. The product of maltotriose was obtained by drying the precipitate at 80 °C for 2 h. The content of maltotriose in the product and the yield of maltotriose were 93.5% (w/w) and 87.3% (w/w), respectively. Results of experiments indicated that this was a promising way of preparation of maltotriose.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Wako K, Hashimoto S, Kubomura S, Yokota K, Aikawa K, Kanaeda J (1979) Purification and some properties of a maltotriose-producing amylase. J Jpn Soc Starch Sci 26:175–181
Takasaki Y (1985) An amylase producing maltotriose from Bacillus subtilis. Agric Biol Chem 49:1091–1097
Takasaki Y, Kitajima M, Tsuruta T, Nonoghchi M, Hayashi S, Imada K (1991) Maltotriose-producing amylase from Microbacterium imperiale. Agric Biol Chem 55:687–692
Ratanakhanokchai K, Kaneko J, Kamio Y, Izaki K (1992) Purification and properties of a maltotetraose and maltotriose-producing amylase from Chloroflexus aurantiacus. Appl Environ Microbiol 58:2490–2494
Kobayashi T, Kanai H, Hayashi T, Akiba T, Akaboshi R, Horikoshi K (1992) Haloalkaliphilic maltotriose-forming α-amylase from the Archaebacterium Natronococcus sp. Strain Ah-36. J Bacteriol 174:3439–3444
Satoh E, Uchimura T, Kudo T, Komagata K (1997) Purification, characterization, and nucleotide sequence of an intracellular maltotriose-producing-amylase from Streptococcus bovis 148. Appl Environ Microbiol 63:4941–4944
Saha BC, Zeikus JG (1989) Novel highly thermostable pullulanase from thermophiles. Trends Biotechnol 7:234–239
Leathers TD (1993) Substrate regulation and specificity of amylases from Aureobasidium strain NRRL Y-12, 974. FEMS Microbiol Lett 110:217–222
Abdulla M, French D (1966) Reverse action of pullulanase. Nature 210:200
Nelson N (1944) A photometric adaptation of the Somogyi method for the determination of glucose. J Bio Chem 153:375–380
Anon (1984) In: Handbook of food analysis (Parts II, III, IV), ISI, New Delhi, p 18
Sawardeker JS, Sloneker SH, Jeanes A (1965) Quantitative determination of monosaccharides as their alditol acetates by gas liquid chromatography. Anal Chem 37:1602–1604
Roy A, Messaoud EB, Bejar S (2003) Isolation and purification of an acidic pullulanase type II from newly isolated Bacillus sp. US149. Enzyme Microb Tech 33:720–724
Kim CH, Nashiru O, Ko JH (1996) Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24 [J]. FEMS Microbiol Lett 138:147–152
Kriegshauser G, Liebl W (2000) Pullulanase from the hyperthermophilic bacterium Thermotoga maritima: purification by β-cyclodextrin affinity chromatography [J]. J Chromatogr B 737:245–251
Kuroiwa T, Shoda H, Ichikawa S, Sato S, Mukataka S (2005) Immobilization and stabilization of pullulanase from Klebsiella pneumoniae by a multipoint attachment method using activated agar gel supports [J]. Process Biochem 40:2637–2642
Swamy MV, Seenayya G (1996) Thermostable pullulanase and α-amylase activity from Clostridium thermosulfurogenes SV9-Optmization of culture conditions for enzyme production [J]. Process Biochem 31:157–162
Messaoud EB, Ammar YB, Mellouli L, Bejar S (2002) Thermostable pullulanase type I from new isolated Bacillus thermoleovorans US105: cloning, sequencing and expression of the gene in E. coli [J]. Enzyme Microb Tech 31:827–832
Kuriki T, Park JH, Imanaka T (1990) Characteristics of thermostable pullulanase from Bacillus stearothermophilus and the nucleotide sequence of the gene [J]. J Ferment Bioeng 69:204–210
Badal C, Saha J, Zeikus G (1989) Novel highly thermostable pullulanase from thermophiles [J]. Trends Biotechnol 7:234–239
Acknowledgments
This research was supported by national high technology research and development program of china (863) (No. 2007AA10Z362), national high technology research and development program of China (Grant No. 2007AA10Z362), national high technology R & D. program of China (Grant No. 2006AA10Z333), Jiangsu provincial natural science foundation (Grant No. BK2008003) and Research Program of State Key Laboratory of Food Science and Technology, Jiangnan University (Project No. SKLF-MB-200804).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Wu, S., Chen, H., Tong, Q. et al. Preparation of maltotriose by hydrolyzing of pullulan with pullulanase. Eur Food Res Technol 229, 821–824 (2009). https://doi.org/10.1007/s00217-009-1118-9
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00217-009-1118-9