ArticleMicrobial cell factories2019
Production of L-alanyl-L-glutamine by immobilized Pichia pastoris GS115 expressing α-amino acid ester acyltransferase.
Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 16 citations in OpenAlex.
- Functional Dipeptide Production by Immobilized Enzyme on Yeast Cell Surface.Journal of microbiology and biotechnology · 2026Article
- Article
- Biosynthesis, Characterization, and Bioactivity of L-Alanyl-L-tyrosine in Promoting Melanin Synthesis.Applied biochemistry and biotechnology · 2024Article
- Immobilization ofIranian journal of microbiology · 2022Article
- Bioproduced Proteins On Demand (Bio-POD) in hydrogels usingBioactive materials · 2021Article
- Magnetic Immobilization ofNanomaterials (Basel, Switzerland) · 2020Article
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7 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundL-Alanyl-L-glutamine (Ala-Gln) represents the great application potential in clinic due to the unique physicochemical properties. A new approach was developed to synthesize Ala-Gln by recombinant Escherichia coli OPA, which could overcome the disadvantages of traditional chemical synthesis. Although satisfactory results had been obtained with recombinant E. coli OPA, endotoxin and the use of multiple antibiotics along with toxic inducer brought the potential biosafety hazard for the clinical application of Ala-Gln.
resultsIn this study, the safer host Pichia pastoris was applied as an alternative to E. coli. A recombinant P. pastoris (named GPA) with the original gene of α-amino acid ester acyltransferase (SsAet) from Sphingobacterium siyangensis SY1, was constructed to produce Ala-Gln. To improve the expression efficiency of SsAet in P. pastoris, codon optimization was conducted to obtain the strain GPAp. Here, we report that Ala-Gln production by GPAp was approximately 2.5-fold more than that of GPA. The optimal induction conditions (cultivated for 3 days at 26 °C with a daily 1.5% of methanol supplement), the optimum reaction conditions (28 °C and pH 8.5), and the suitable substrate conditions (AlaOMe/Gln = 1.5/1) were also achieved for GPAp. Although most of the metal ions had no effects, the catalytic activity of GPAp showed a slight decrease in the presence of Fe
conclusionsCharacterized by economy, efficiency and practicability, production of Ala-Gln by recycling immobilized GPAp (whole-cell biocatalyst) is represents a green and promising way in industrial.
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