Skip to main content

Immobilized l-aspartate ammonia-lyase from Bacillus sp. YM55-1 as biocatalyst for highly concentrated l-aspartate synthesis

Cárdenas-Fernández, Max, López, Carmen, Álvaro, Gregorio, López-Santín, Josep (2012) Immobilized l-aspartate ammonia-lyase from Bacillus sp. YM55-1 as biocatalyst for highly concentrated l-aspartate synthesis. Bioprocess and Biosystems Engineering, 35 . pp. 1437-1444. ISSN 1615-7591. E-ISSN 1615-7605. (doi:10.1007/s00449-012-0732-2) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:88153)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
https://doi.org/10.1007/s00449-012-0732-2

Abstract

L-Aspartate ammonia-lyase from Bacillus sp. YM55-1 (AspB, EC 4.3.1.1) catalyzes the reversible conversion of L-aspartate (Asp) into fumarate and ammonia with a high specific activity toward the substrate. AspB was expressed in Escherichia coli and partially purified by heat precipitation and saturation with ammonium sulfate reaching purification factor of 7.7 and specific activity of 334 U/mg of protein. AspB was immobilized by covalent attachment on Eupergit® C (epoxy support) and MANA-agarose (amino support), and entrapment in LentiKats® (polyvinyl alcohol) with retained activities of 24, 85 and 63 %, respectively. Diffusional limitations were only observed for the enzyme immobilized in LentiKats® and were overcome by increasing substrate concentration. Free and immobilized AspB were used for the synthesis of aspartate achieving high product concentration (≥450 mM) after 24 h of reaction. Immobilized biocatalysts were efficiently reused in 5 cycles of Asp synthesis, keeping over 90 % of activity and reaching over 90 % of conversion in all the cases.

Item Type: Article
DOI/Identification number: 10.1007/s00449-012-0732-2
Uncontrolled keywords: Enzymatic L-aspartate synthesis; L-Aspartate ammonia-lyase immobilization; Eupergit® C; MANA-agarose; LentiKats®
Subjects: Q Science > QP Physiology (Living systems)
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Max Cardenas Fernandez
Date Deposited: 14 May 2021 15:19 UTC
Last Modified: 10 Jun 2021 15:34 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/88153 (The current URI for this page, for reference purposes)
Cárdenas-Fernández, Max: https://orcid.org/0000-0003-1422-5369
  • Depositors only (login required):