期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 1, 页码 -出版社
MDPI
DOI: 10.3390/ijms21010091
关键词
LaSGNH1; Lactobacillus acidophilus; SGNH family esterases; immobilization; crosslinked enzyme aggregates
资金
- National Research Foundation of Korea - Korean Government [NRF-2018R1D1A1B07044447]
- National Research Foundation of Korea [2018R1D1A1B07044447] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The SGNH family esterases are highly effective biocatalysts due to their strong catalytic efficiencies, great stabilities, relatively small sizes, and ease of immobilization. Here, a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus NCFM, which has homologues in many Lactobacillus species, was identified, characterized, and immobilized. LaSGNH1 is highly active towards acetate- or butyrate-containing compounds, such as p-nitrophenyl acetate or 1-naphthyl acetate. Enzymatic properties of LaSGNH1, including thermal stability, optimum pH, chemical stability, and urea stability, were investigated. Interestingly, LaSGNH1 displayed a wide range of substrate specificity that included glyceryl tributyrate, tert-butyl acetate, and glucose pentaacetate. Furthermore, immobilization of LaSGNH1 by crosslinked enzyme aggregates (CLEAs) showed enhanced thermal stability and efficient recycling property. In summary, this work paves the way for molecular understandings and industrial applications of a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus.
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