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Application of Invertase Immobilized on Chitosan Using Glutaraldehyde or Tris(Hydroxymethyl)Phosphine as Cross-Linking Agent to Produce Bioethanol

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Abstract

Invertase was immobilized on chitosan using glutaraldehyde or tris(hydroxymethyl)phosphine as cross-linker. The optimum pH for free and immobilized enzyme was found to be 4.5 and 5.5, respectively. The optimum hydrolysis temperature was 55 °C for both the free and immobilized forms. Km and Vmax values for free invertase, and invertase immobilized on glutaraldehyde- and THP-activated chitosan were 15, 19, and 20 mM, respectively, and 238, 204, and 212 mM min−1, respectively. The THP-immobilized enzyme had the highest pH and thermal stability, higher reusability with 70% retention in activity after 9 batches of reuse and higher storage stability with 90% retention in activity after 12 weeks at 4 °C, pH 4.5. Fermentation of cane molasses by yeast to form ethanol in the presence of free invertase at 30°C, pH 5.0 led to an increase in ethanol production by 3% and the production increased by 10.7% when immobilized invertase was used as catalyst.

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Funding

This research was financially supported by the University Grant Commission (Government of India).

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Authors and Affiliations

  1. Department of Biosciences, Jamia Millia Islamia, New Delhi, India

    Ishita Malhotra & Seemi Farhat Basir

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  1. Ishita Malhotra
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  2. Seemi Farhat Basir
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Correspondence to Seemi Farhat Basir.

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Highlights

• Invertase from Saccharomyces cerevisiae was immobilized on chitosan.

• Glutaraldehyde and tris(hydroxymethyl)phosphine were compared as cross-linking agents.

• Immobilization using THP as cross-linker increased pH and thermal stability of invertase.

• Invertase immobilized with THP cross-linker was used for bioethanol production from cane molasses.

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Malhotra, I., Basir, S.F. Application of Invertase Immobilized on Chitosan Using Glutaraldehyde or Tris(Hydroxymethyl)Phosphine as Cross-Linking Agent to Produce Bioethanol. Appl Biochem Biotechnol 191, 838–851 (2020). https://doi.org/10.1007/s12010-019-03162-3

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  • DOI: https://doi.org/10.1007/s12010-019-03162-3

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