Efficient substrate accessibility of cross-linked levanase aggregates using dialdehyde starch as a macromolecular cross-linker

Noor Hidayah Abd Rahman; Nardiah Rizwana Jaafar; Nur Arbainah Shamsul Annuar; Roshanida A Rahman; Abdul Munir Abdul Murad; Hesham Ali El-Enshasy; Rosli Md Illias

doi:10.1016/j.carbpol.2021.118159

Efficient substrate accessibility of cross-linked levanase aggregates using dialdehyde starch as a macromolecular cross-linker

Carbohydr Polym. 2021 Sep 1:267:118159. doi: 10.1016/j.carbpol.2021.118159. Epub 2021 May 7.

Authors

Noor Hidayah Abd Rahman¹, Nardiah Rizwana Jaafar¹, Nur Arbainah Shamsul Annuar², Roshanida A Rahman¹, Abdul Munir Abdul Murad³, Hesham Ali El-Enshasy⁴, Rosli Md Illias⁵

Affiliations

¹ Department of Bioprocess Engineering, School of Chemical and Energy Engineering, Faculty of Engineering, Universiti Teknologi Malaysia, 81300, Skudai, Johor Bahru, Johor Darul Takzim, Malaysia.
² Health and Wellness Research Alliance, Universiti Teknologi Malaysia, 81300, Skudai, Johor Bahru, Johor Darul Takzim, Malaysia.
³ School of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Malaysia.
⁴ Institute of Bioproduct Development, Universiti Teknologi Malaysia, 81310 Skudai, Johor, Malaysia.
⁵ Department of Bioprocess Engineering, School of Chemical and Energy Engineering, Faculty of Engineering, Universiti Teknologi Malaysia, 81300, Skudai, Johor Bahru, Johor Darul Takzim, Malaysia; Health and Wellness Research Alliance, Universiti Teknologi Malaysia, 81300, Skudai, Johor Bahru, Johor Darul Takzim, Malaysia; Institute of Bioproduct Development, Universiti Teknologi Malaysia, 81310 Skudai, Johor, Malaysia. Electronic address: r-rosli@utm.my.

PMID: 34119133
DOI: 10.1016/j.carbpol.2021.118159

Abstract

Cross-linked enzyme aggregates (CLEAs) are influenced by mass diffusion limitations such as the degree of molecular cross-linking attained, which affects substrate accessibility. Thus, this study seeks to improve substrate accessibility using macromolecular cross-linkers in cross-linked levanase aggregates (CLLAs) formation for levan-type fructooligosaccharides (L-FOS) production. Dialdehyde starch-tapioca (DAST) was successfully developed and used to cross-link levanase to form CLLAs-D and with bovine serum albumin (BSA) to form CLLAs-DB which showed activity recoveries of 65.6% and 81.6%, respectively. After cross-linking, the pH (6-10) and thermal stability (30-40 °C) increased, and organic solvent tolerance resulted in the activation of CLLAs. Likewise, CLLAs-DB had higher substrate affinity and accessibility and a higher effectiveness factors than CLLAs-D. The total L-FOS yield of CLLAs-DB (78.9% (w/v)) was higher than that of CLLAs-D (62.4% (w/v)). Therefore, as a cross-linker, DAST may have application prospects as a promising and green biocatalyst for product formation.

Keywords: Dialdehyde starch; Fructooligosaccharides; Levanase; Macromolecular cross-linked enzyme aggregates; Tapioca.