The Acyl-CoA Binding Protein Affects Pigment Production in CICC41233

Overview

Journal 3 Biotech

Publisher Springer

Specialty Biotechnology

Date 2018 Feb 13

PMID 29430382

Citations 5

Authors

Chuannan Long

Mengmeng Liu

Xia Chen

Xiaofang Wang

Mingqiang Ai

Jingjing Cui

Bin Zeng

Affiliations

Soon will be listed here.

Abstract

The present study verified whether acyl-coenzyme A (acyl-CoA)-binding protein (ACBP) affected the production of pigments (MPs) in CICC41233 (MrACBP). Phylogenetic analysis revealed that the cloned gene, which encoded the MrACBP protein, exhibited the closest match (99% confidence level) to the gene from . The MrACBP and maltose-binding protein (MBP) were simultaneously expressed in Rosetta DE3 in the form of a fusion protein. The microscale thermophoresis binding assay revealed that the purified MBP-MrACBP exhibited a higher affinity for myristoyl-CoA (Kd = 88.16 nM) than for palmitoyl-CoA (Kd = 136.07 nM) and octanoyl-CoA (Kd = 270.9 nM). Further, the gene was homologously overexpressed in CICC41233, and a positive transformant ACBP5 was isolated. The fatty acid myristic acid in ACBP5 was lower than that in the parent strain CICC41233. However, when compared with the parent strain, the production of total MPs, water-soluble pigment, and ethanol-soluble pigment in ACBP5 increased by 11.67, 9.80, and 12.70%, respectively, after 6 days. The relative gene expression level, as determined by a quantitative real-time polymerase chain reaction analysis, of the key genes , , , , and increased by 4.03-, 3.58-, 1.67-, 2.11-, and 2.62-fold after 6 days. These data demonstrate the binding preference of MrACBP for myristoyl-CoA, and its influence on MPs production.

Citing Articles

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