Covalent immobilization of Bacillus subtilis lipase A on Fe3O4 nanoparticles by aldehyde tag: An ideal immobilization with minimal chemical modification

Lyu, Jiabao; Li, Zidan; Men, Juncheng; Jiang, Ruyun; Tang, Guilin; Zhou, Ye; Gao, Renjun

doi:10.1016/j.procbio.2019.03.017

Cited by 26 publications

(14 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ST2570 immobilized on resin D380 (Figure 5a) retained 40% activity after eight cycles, and the ST0779 immobilized on SiO 2 -Fe 3 O 4 -NP ( Figure 5c) retained 80% activity after eight cycles. Compared with BsLA immobilized on SiO 2 -Fe 3 O 4 -NP ( Figure 5d) [29] and ST2570 immobilized on SBA-15 ( Figure 5b) [28], BsLA and ST0779 immobilized on SiO 2 -Fe 3 O 4 -NP could maintain higher activity after eight recycles. However, the activity of ST2570 with resin D380 or SBA-15 as the immobilized carrier decreased significantly after five cycles.…”

Section: Immobilization Efficiency and Activity Recovery Ratementioning

confidence: 93%

“…In our previous reports, Jian et al immobilized ST2570 to SBA-15 modified with amino group [28] and Lyu et al immobilized BsLA to Fe 3 O 4 magnetic nanoparticles covered with amino-modified SiO 2 (SiO 2 -Fe 3 O 4 -NP) using this site-specific immobilization method [29]. In order to further confirm the universality of this method for the immobilization of enzymes, we chose styrene anion exchange resin (D380) and Fe 3 O 4 magnetic nanoparticles as the immobilized carriers.…”

Section: Immobilization Efficiency and Activity Recovery Ratementioning

confidence: 99%

“…Three enzymes were chosen as models. They were thermophilic acyl aminopeptidase (EC 3.4.19.1) from Sulfolobus tokodaii (ST0779), thermophilic dehalogenase (EC 3.8.1.2) from Sulfolobus tokodaii (ST2570) [28], and Lipase A (EC 3.1.1.3) from Bacillus subtilis (BsLA) [29]. Afterward, we covalently linked aldehyde-tagged enzymes to different amino-modified carriers and characterized several properties.…”

Section: Introductionmentioning

confidence: 99%

“…The activity recovery rate and immobilization efficiency of BsLA immobilized by SiO 2 -Fe 3 O 4 -NP[29]. The activity recovery rate and immobilization efficiency of ST0779 immobilized by SiO 2 -Fe 3 O 4 -NP.…”

mentioning

confidence: 98%

“…The reutilization of the immobilized enzyme. (a) The number of reuses of ST2570 immobilized by resin D380; (b) the number of reuses of ST2570 immobilized by SBA-15 [28]; (c) the number of reuses of ST0779 immobilized by Fe 3 O 4 covered with SiO2; (d) the number of reuses of BsLA immobilized by Fe 3 O 4 covered with SiO 2[29].…”

mentioning

confidence: 99%

See 4 more Smart Citations

Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization

Wang

Jian

et al. 2020

Catalysts

Self Cite

View full text Add to dashboard Cite

In recent years, the development and application of site-specific immobilization technology for proteins have undergone significant advances, which avoids the unwanted and random covalent linkage between the support and active site of protein in the covalent immobilization. Formylglycine generating enzyme (FGE) can transform the cysteine from a conversed 6-amino-acid sequence CXPXR into formylglycine with an aldehyde group (also termed as “aldehyde tag”). Based on the frame of pET-28a, the His-tags were replaced with aldehyde tags. Afterward, a set of plasmids were constructed for site-specific covalent immobilization, their His-tags were knock out (DH), or were replaced at different positions: N-terminal (NQ), C-terminal (CQ), or both (DQ) respectively. Three different enzymes, thermophilic acyl aminopeptidase (EC 3.4.19.1) from Sulfolobus tokodaii (ST0779), thermophilic dehalogenase (EC 3.8.1.2) from Sulfolobus tokodaii (ST2570), and Lipase A (EC 3.1.1.3) from Bacillus subtilis (BsLA) were chosen as model enzymes to connect with these plasmid systems. The results showed that different aldehyde-tagged enzymes can be successfully covalently attached to different carriers modified with an amino group, proving the universality of the method. The new immobilized enzyme also presented better thermostability and reutilization than those of the free enzyme.

show abstract

Section: Immobilization Efficiency and Activity Recovery Ratementioning

confidence: 93%

Section: Immobilization Efficiency and Activity Recovery Ratementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 98%

mentioning

confidence: 99%

See 3 more Smart Citations

Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization

Wang

Jian

et al. 2020

Catalysts

Self Cite

View full text Add to dashboard Cite

show abstract

Lipase‐Immobilized Magnetic Nanoparticles: Promising Nanobiocatalysts for Biodiesel Production

Touqeer

Mumtaz

Mukhtar

2021

Nano‐ and Biocatalysts for Biodiesel Production

View full text Add to dashboard Cite

Design and characterization of a chimeric alginate lyase for immobilization to produce well‐defined oligosaccharides

Zhang

Lyu

Liu

et al. 2022

Food Bioengineering

View full text Add to dashboard Cite

Recently, a novel two-domain alginate lyase (AlyAL01) was cloned from Algibacter sp. and successfully overexpressed in Escherichia coli BL21(DE3). Biochemical analysis showed that the N-terminal carbohydrate-binding module (CBM) of AlyAL01 had no effect on the enzyme activity and product distributions. Therefore, the N-terminal CBM was substituted with CBM3 to confer the designed chimeric protein with the ability to specifically bind to regenerated amorphous cellulose. As anticipated, the designed chimeric protein (CBM3-L1) exhibited a similar enzyme activity. Moreover, it was found that the CBM3-L1 combined the purification and immobilization in one step with high immobilized efficiency of 65.8%. The immobilized enzyme exhibited good storage stability and moderate reusability. The immobilized enzyme could keep 85% activity when incubated at 4°C for 60 days and 70% activity when incubated at 25°C for 30 days. Furthermore, the immobilized CBM3-L1 kept about 50% of its initial activity after being reused five times. Finally, immobilized CBM3-L1 successively produced well-defined alginate oligosaccharides (AOS) with DPs of 2-6 by controlling reaction time. In sum, our current study provided a feasible strategy for well-defined AOS production.K E Y W O R D S alginate lyase, alginate oligosaccharides, cellulose-binding domain, immobilized enzyme

show abstract

Covalent immobilization of Bacillus subtilis lipase A on Fe3O4 nanoparticles by aldehyde tag: An ideal immobilization with minimal chemical modification

Cited by 26 publications

References 34 publications

Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization

Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization

Lipase‐Immobilized Magnetic Nanoparticles: Promising Nanobiocatalysts for Biodiesel Production

Design and characterization of a chimeric alginate lyase for immobilization to produce well‐defined oligosaccharides

Contact Info

Product

Resources

About