期刊
CARBOHYDRATE POLYMERS
卷 267, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.carbpol.2021.118159
关键词
Dialdehyde starch; Tapioca; Levanase; Macromolecular cross-linked enzyme aggregates; Fructooligosaccharides
资金
- Universiti Teknologi Malaysia (UTM) [PY/2017/01569, Q. J13000.2509.18H72]
The study focuses on improving substrate accessibility by forming cross-linked levanase aggregates (CLLAs) using a cross-linker, Dialdehyde starch-tapioca (DAST), for levan-type fructooligosaccharides (L-FOS) production. CLLAs-D and CLLAs-DB were successfully developed, with CLLAs-DB showing higher substrate affinity and accessibility, resulting in a higher total L-FOS yield compared to CLLAs-D.
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 degrees 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.
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