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Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFMopen access

Authors
Ly Thi Huong Luu LeYoo, WankiJeon, SangeunKim, Kyeong KyuKim, T. Doohun
Issue Date
Jan-2020
Publisher
MDPI
Keywords
LaSGNH1; Lactobacillus acidophilus; SGNH family esterases; immobilization; crosslinked enzyme aggregates
Citation
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.21, no.1
Journal Title
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume
21
Number
1
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/2578
DOI
10.3390/ijms21010091
ISSN
1661-6596
1422-0067
Abstract
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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