Biotechnology & Applied Microbiology

Magnetic micro-macro biocatalysts applied to industrial bioprocesses

Authors: Del Arco, J; Alcantara, AR; Fernandez-Lafuente, R; Fernandez-Lucas, J

Article.
Bioresour. Technol. vol: 322. page: 1873-2976
Date: feb. 2021.
Doi: 10.1016/j.biortech.2020.124547.

Abstract:
The use of magnetic biocatalysts is highly beneficial in bioprocesses technology, as it allows their easy recovering and enhances biocatalyst lifetime. Thus, it simplifies operational processing and increases efficiency, leading to more cost-effective processes. The [read more]

Molecular characterization and heterologous expression of two alpha-glucosidases from Metschnikowia spp, both producers of honey sugars

Authors: Garcia-Gonzalez, M; Minguet-Lobato, M; Plou, FJ; Fernandez-Lobato, M

Article.
Microb. Cell. Fact.. vol: 19. page: .
Date: jul-11. 2020.
Doi: 10.1186/s12934-020-01397-y.

Abstract:
Background: alpha-Glucosidases are widely distributed enzymes with a varied substrate specificity that are traditionally used in biotechnological industries based on oligo- and polysaccharides as starting materials. According to amino acid sequence homology, alpha-glucosidases are included into two major families, [read more]

Modulating the properties of the lipase from Thermomyces lanuginosus immobilized on octyl agarose beads by altering the immobilization conditions

Authors: Lokha, Y; Arana-Pena, S; Rios, NS; Mendez-Sanchez, C; Goncalves, LRB; Lopez-Gallego, F; Fernandez-Lafuente, R

Article.
Enzyme Microb. Technol.. vol: 133. page: 0141-0229.
Date: FEB. 2020.
Doi: 10.1016/j.enzmictec.2019.109461.

Abstract:
The lipase from Thermomyces lanuginosus (TLL) has been immobilized on octyl-agarose beads via interfacial activation under 16 different conditions (changing the immobilization pH, the ionic strength, the presence of additives like calcium, phosphate [read more]

Pectin lyase immobilization using the glutaraldehyde chemistry increases the enzyme operation range

Authors: Dal Magro, L; Kornecki, JF; Klein, MP; Rodrigues, RC; Fernandez-Lafuente, R

Article.
Enzyme Microb. Technol.. vol: 132. page: 0141-0229.
Date: JAN. 2020.
Doi: 10.1016/j.enzmictec.2019.109397.

Abstract:
Pectin lyase (from Rohapect 10 L) was immobilized on glutaraldehyde supports at low ionic strength at pH 5, 6.5 or 8 and later incubated at pH 8 for 48 h. The activity recovery of the biocatalysts [read more]

Prolongation of secondary drying step of phospholipid lyophilization greatly improves acidolysis reactions catalyzed by immobilized lecitase ultra

Authors: Verdasco-Martin, CM; Corchado-Lopo, C; Fernandez-Lafuente, R; Otero, C

Article.
Enzyme Microb. Technol.. vol: 132. page: 0141-0229.
Date: JAN. 2020.
Doi: 10.1016/j.enzmictec.2019.109388.

Abstract:
Conjugated linolenic acid (CLA) has important health effects, and their phospholipids forms (PL) are advantageous vehicles of this bioactive agent. Acidolysis of soybean phosphatidylcholine (PC) with conjugated linolenic acid (CLA) catalyzed by Lecitase (R) Ultra immobilized on Duolite A658 [read more]

Modulating the properties of the lipase from Thermomyces lanuginosus immobilized on octyl agarose beads by altering the immobilization conditions

Authors: Lokha, Y; Arana-Pena, S; Rios, NS; Mendez-Sanchez, C; Goncalves, LRB; Lopez-Gallego, F; Fernandez-Lafuente, R

Article.
Enzyme Microb. Technol.. vol: 133. page: 0141-0229.
Date: FEB. 2020.
Doi: 10.1016/j.enzmictec.2019.109461.

Abstract:
The lipase from Thermomyces lanuginosus (TLL) has been immobilized on octyl-agarose beads via interfacial activation under 16 different conditions (changing the immobilization pH, the ionic strength, the presence of additives like calcium, phosphate [read more]

Pectin lyase immobilization using the glutaraldehyde chemistry increases the enzyme operation range

Authors: Dal Magro, L; Kornecki, JF; Klein, MP; Rodrigues, RC; Fernandez-Lafuente, R

Article.
Enzyme Microb. Technol.. vol: 132. page: 0141-0229.
Date: JAN. 2020.
Doi: 10.1016/j.enzmictec.2019.109397.

Abstract:
Pectin lyase (from Rohapect 10 L) was immobilized on glutaraldehyde supports at low ionic strength at pH 5, 6.5 or 8 and later incubated at pH 8 for 48 h. The activity recovery of the biocatalysts [read more]

Prolongation of secondary drying step of phospholipid lyophilization greatly improves acidolysis reactions catalyzed by immobilized lecitase ultra

Authors: Verdasco-Martin, CM; Corchado-Lopo, C; Fernandez-Lafuente, R; Otero, C

Article.
Enzyme Microb. Technol.. vol: 132. page: 0141-0229.
Date: JAN. 2020.
Doi: 10.1016/j.enzmictec.2019.109388.

Abstract:
Conjugated linolenic acid (CLA) has important health effects, and their phospholipids forms (PL) are advantageous vehicles of this bioactive agent. Acidolysis of soybean phosphatidylcholine (PC) with conjugated linolenic acid (CLA) catalyzed by Lecitase (R) Ultra immobilized on Duolite A658 [read more]

Stabilization of dimeric beta-glucosidase from Aspergillus niger via glutaraldehyde immobilization under different conditions

Authors: Vazquez-Ortega, PG; Alcaraz-Fructuoso, MT; Rojas-Contreras, JA; Lopez-Miranda, J; Fernandez-Lafuente, R

Article.
Enzyme Microb. Technol.. vol: 110. page: 0141-0229.
Date: MAR. 2018.
Doi: 10.1016/j.enzmictec.2017.12.007.

Abstract:
The dimeric enzyme beta-glucosidase from Aspergillus niger has been immobilized on different amino-agarose beads at pH 5 and 7, exploiting the versatility of glutaraldehyde. The stability of the free enzyme depended on enzyme concentration. Immobilization via ion [read more]

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