Co-encapsulation of amyloglucosidase with starch and Saccharomyces cerevisiae as basis for a long-lasting CO2 release
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CO2 is known as a major attractant for many arthropod pests which can be exploited for pest control within novel attract-and-kill strategies. This study reports on the development of a slow-release system for CO2 based on calcium alginate beads containing granular corn starch, amyloglucosidase and Saccharomyces cerevisiae. Our aim was to evaluate the conditions which influence the CO2 release and to clarify the biochemical reactions taking place within the beads. The amyloglucosidase was immobilized with a high encapsulation efficiency of 87% in Ca-alginate beads supplemented with corn starch and S. cerevisiae biomass. The CO2 release from the beads was shown to be significantly affected by the concentration of amyloglucosidase and corn starch within the beads as well as by the incubation temperature. Beads prepared with 0.1 amyloglucosidase units/g matrix solution led to a long-lasting CO2 emission at temperatures between 6 and 25 °C. Starch degradation data correlated well with the CO2 release from beads during incubation and scanning electron microscopy micrographs visualized the degradation of corn starch granules by the co-encapsulated amyloglucosidase. By implementing MALDI-ToF mass spectrometry imaging for the analysis of Ca-alginate beads, we verified that the encapsulated amyloglucosidase converts starch into glucose which is immediately consumed by S. cerevisiae cells. When applied into the soil, the beads increased the CO2 concentration in soil significantly. Finally, we demonstrated that dried beads showed a CO2 production in soil comparable to the moist beads. The long-lasting CO2-releasing beads will pave the way towards novel attract-and-kill strategies in pest control.
KeywordsAlginate beads Attract-and-kill Baker’s yeast Carbon dioxide Co-immobilization Glucoamylase Slow-release
We would like to thank T. Dellweg from Deutsche Hefewerke GmbH (Nürnberg, Germany) for providing baker’s yeast strain S. cerevisiae H205.
This study was supported by means of the German Federal Ministry of Food and Agriculture (BMEL) as part of the project ATTRACT (No. 2814701811).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest. The authors alone are responsible for the content and writing of the paper.
- FAO (2002) Compendium addendum 10/FNP 52 Add.10/9 vol 1/93Google Scholar
- Giordano RLC, Trovati J, Schmidell W (2008) Continuous production of ethanol from starch using glucoamylase and yeast co-immobilized in pectin gel. Appl Biochem. Biotech 147:47–61Google Scholar
- Hou H-P, Yan Y-W (2009) Co-immobilization of glucoamylase and yeast by adsorption-embedment method. Food Sci 30:201–204Google Scholar
- Li PH, Weiser CJ, Van Huystee R (1965) Changes in metabolites of red-osier dogwood during cold acclimation. J Amer Soc Hort Sci 86:723–730Google Scholar
- Mansfeld J, Dautzenberg H (1997) Coimmobilization of enzymes and cells. In: Bickerstaff GF (ed) Immobilization of enzymes and cells. Humana Press, New Jersey, pp 319–326Google Scholar
- McGhee JE, Carr ME, Stjulian G (1984) Continuous bioconversion of starch to ethanol by calcium-alginate immobilized enzymes and yeasts. Cereal Chem 61:446–449Google Scholar
- Morris VJ, Gunning AP, Faulds CB, Williamson G, Svensson B (2005) AFM images of complexes between amylose and Aspergillus niger glucoamylase mutants, native, and mutant starch binding domains: a model for the action of glucoamylase. Starch-Stärke 57:1–7Google Scholar
- Robyt JF (2009) Enzymes and their action on starch. In: BeMiller JN, Whistler RL (eds) Starch chemistry and technology. Academic, London, pp 237–292Google Scholar
- Shetty RM, Lineback DR, Seib PA (1974) Determining the degree of starch gelatinization. Cereal Chem 51:364–375Google Scholar