3 Biotech

, 8:169 | Cite as

Optimization of hydrolysis conditions for the mannooligosaccharides copra meal hydrolysate production

  • Jurairat Rungruangsaphakun
  • Suttipun Keawsompong
Original Article


Copra meal is a good source of galactomannan and its mannooligosaccharides have prebiotic properties. However, limited data are available concerning the ideal requirements for mannan hydrolysis. Thus, optimum hydrolysis conditions for the production of oligosaccharides from copra meal hydrolysate were investigated using response surface methodology. Model validation provided good agreement between experimental results and predicted responses. Maximum oligosaccharide of 14.41 ± 0.09 mg/ml (20 ml) was obtained at an enzyme concentration of 16.52 U/ml, substrate concentration 15% and reaction time 12 h. On a larger scale, this increased to 15.76 ± 0.04 mg/ml (200 ml) and 16.89 mg/ml (2000 ml). Defatted copra meal hydrolysate promoted the growth of beneficial bacteria as lactobacilli and bifidobacteria, while inhibiting pathogens Salmonella serovar Enteritidis S003, Escherichia coli E010, Staphylococcus aureus TISTR 029 and Shigella dysenteriae DMST 1511. Higher yield of oligosaccharides under optimum conditions indicated the potential of this method for production of mannooligosaccharides from copra meal hydrolysate on an industrial scale.


Mannooligosaccharides Defatted copra meal Hydrolysis conditions Response surface methodology 



This research was financially supported by the Graduate School of Kasetsart University and the National Research Council of Thailand.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest in the publication.


  1. Balasubramaniam K (1976) Polysaccharides of the kernel of maturing and mature coconuts. J Food Sci 41:1370–1373CrossRefGoogle Scholar
  2. Chandrakant P, Bisaria VS (1998) Simultaneous bioconversion of cellulose and hemicellulose to ethanol. Crit Rev Biotechnol 18:295–331CrossRefGoogle Scholar
  3. Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350–356CrossRefGoogle Scholar
  4. Gübitz GM, Hayn M, Ürbanz G, Steiner W (1996) Purification and properties of an acidic β-mannanase from Sclerotium rolfsii. J Biotechnol 45(2):165–172CrossRefGoogle Scholar
  5. Hashimoto Y, Fukumoto J (1969) Studies on the enzyme treatment of coffee beans. Nippon Nogeikagaku Kaishi 43:317–322CrossRefGoogle Scholar
  6. Index Mundi (2014) IndexMundi country reports, Massachusetts. Accessed 13 Jul 2014
  7. Line JESB, Cox NA, Stern NJ (1997) Yeast treatment to reduce Salmonella and Campylobacter, populations associated with broiler chickens subjected to transport stress. Poult Sci 76:1227–1231CrossRefGoogle Scholar
  8. Marcos SB, Valeria RP, Dalva CR, Sonia MCD (1995) Seed galactomannan in the classification and evolution of the Leguminosae. Phytochem 38:871–875CrossRefGoogle Scholar
  9. McCleary VB, Matheson NK (1974) Galactomannan structure and β-mannanase and β-mannosidase activity in germinating legume seeds. Phytochemistry 14:1187–1194CrossRefGoogle Scholar
  10. Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428CrossRefGoogle Scholar
  11. Moghaddam SS, Moghaddam MRA, Arami M (2010) Coagulation/flocculation process for dye removal using sludge from water treatment plant: optimization through response surface methodology. J Hazard Mater 175:651–657CrossRefGoogle Scholar
  12. Özer A, Gürbüz G, Çalımlı A, Körbahti BK (2009) Biosorption of copper(II) ions on Enteromorpha prolifera: application of response surface methodology (RSM). Chem Eng J 146:377–387CrossRefGoogle Scholar
  13. Pangsri P (2014) Characterization of mannanase from Bacillus circulans NT 6.7 and its application in mannooligosaccharides preparation. Ph.D. thesis, Kasetsart UniversityGoogle Scholar
  14. Pangsri P, Piwpankaew Y, Ingkakul A, Nitisinprasert S, Keawsompong S (2015) Characterization of mannanase from Bacillus circulans NT 6.7 and its application in mannooligosaccharides preparation as prebiotic.
  15. Phothichitto K, Nitisinprasert S, Keawsompong S (2006) Isolation, screening and identification of mannanase producing microorganisms. Kasetsart J (Nat Sci) 40(Suppl):26–38Google Scholar
  16. Piwpankaew Y, Sakulsirirat S, Nitisinprasert S, Ngu-yend TH, Haltrich D, Keawsompong S (2014) Cloning, secretory expression and characterization of recombinant β-mannanase from Bacillus circulans NT 6.7.
  17. Ray S, Pubols MH, Mgginnis J (1982) The effect of a purified guar degrading enzyme on chicken growth. Poult Sci 61:488–494CrossRefGoogle Scholar
  18. Titapoka S, Keawsompong S, Haltrich D, Nitisinprasert S (2008) Selection and characterization of mannanase-producing bacteria useful for the formation of prebiotic manno-oligosaccharides from copra meal. World J Microbiol Biotechnol 24:1425–1433CrossRefGoogle Scholar
  19. Tomotari M (1990) Bifidobacteria and their role in human health. J Ind Microbiol 6:263–268CrossRefGoogle Scholar
  20. Wootton AN, Luker-Brown RJ, Cheetham PSJ (1993) The extraction of a glucomannan polysaccharide from konjac corms (elephant yam, Amorphophallus rivieri). J Sci Food Agric 61:429–433CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Jurairat Rungruangsaphakun
    • 1
  • Suttipun Keawsompong
    • 1
    • 2
  1. 1.Department of Biotechnology, Faculty of Agro-IndustryKasetsart UniversityBangkokThailand
  2. 2.Special Research Unit: Probiotic and Prebiotics for Health, Center for Advanced Studies for Agriculture and Food (CASAF), Institute for Advanced StudiesKasetsart UniversityBangkokThailand

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