ArticlePloS one2016
Surface Immobilization of Human Arginase-1 with an Engineered Ice Nucleation Protein Display System in E. coli.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Whole-cell surface-display system in attenuated Salmonella Enteritidis for slide microagglutination-based antibody detection.Microbial cell factories · 2026Article
- Engineered Bacteria-Vesicle Delivered Lactate Reprogramming Boosts Tumor Radiosensitivity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Development of a starch-fermenting Zymomonas mobilis strain for bioethanol production.Microbial cell factories · 2024Article
- Expression of phenylalanine ammonia lyase as an intracellularly free and extracellularly cell surface-immobilized enzyme on a gut microbe as a live biotherapeutic for phenylketonuria.Science China. Life sciences · 2023Article
- Regulated strategies of cold-adapted microorganisms in response to cold: a review.Environmental science and pollution research international · 2021Review
- Decorating the surface of Escherichia coli with bacterial lipoproteins: a comparative analysis of different display systems.Microbial cell factories · 2021Article
- Simultaneous hydrolysis of carbaryl and chlorpyrifos by Stenotrophomonas sp. strain YC-1 with surface-displayed carbaryl hydrolase.Scientific reports · 2017Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ice nucleation protein (INP) is frequently used as a surface anchor for protein display in gram-negative bacteria. Here, MalE and TorA signal peptides, and three charged polypeptides, 6×Lys, 6×Glu and 6×Asp, were anchored to the N-terminus of truncated INP (InaK-N) to improve its surface display efficiency for human Arginase1 (ARG1). Our results indicated that the TorA signal peptide increased the surface translocation of non-protein fused InaK-N and human ARG1 fused InaK-N (InaK-N/ARG1) by 80.7% and 122.4%, respectively. Comparably, the MalE signal peptide decreased the display efficiencies of both the non-protein fused InaK-N and InaK-N/ARG1. Our results also suggested that the 6×Lys polypeptide significantly increased the surface display efficiency of K6-InaK-N/ARG1 by almost 2-fold, while also practically abolishing the surface translocation of non-protein fused InaK-N, indicating the interesting roles of charged polypeptides in bacteria surface display systems. Cell surface-immobilized K6-InaK-N/ARG1 presented an arginase activity of 10.7 U/OD600 under the optimized conditions of 40°C, pH 10.0 and 1 mM Mn2+, which could convert more than 95% of L-Arginine (L-Arg) to L-Ornithine (L-Orn) in 16 hours. The engineered InaK-Ns expanded the INP surface display system, which aided in the surface immobilization of human ARG1 in E. coli cells.
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