scholarly journals Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase

2010 ◽  
Vol 23 (10) ◽  
pp. 781-787 ◽  
Author(s):  
Hiroyuki Nakai ◽  
Bent O. Petersen ◽  
Yvonne Westphal ◽  
Adiphol Dilokpimol ◽  
Maher Abou Hachem ◽  
...  
Keyword(s):  
Lactobacillus Acidophilus ◽  
Rational Engineering ◽  
Dual Specificity ◽  
Lactobacillus Acidophilus Ncfm ◽  
Maltose Phosphorylase

Crystal Structure of α-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding

2011 ◽  
Vol 412 (3) ◽  
pp. 466-480 ◽  
Author(s):  
Folmer Fredslund ◽  
Maher Abou Hachem ◽  
René Jonsgaard Larsen ◽  
Pernille Gerd Sørensen ◽  
Pedro M. Coutinho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Lactobacillus Acidophilus ◽  
Substrate Binding ◽  
Tetramer Formation ◽  
Lactobacillus Acidophilus Ncfm ◽  
Insight Into

scholarly journals Molecular cloning, expression and adhesion analysis of silent slpB of Lactobacillus acidophilus NCFM

AMB Express ◽  
2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Yuxing Guo ◽  
Xiangyue Li ◽  
Yao Yang ◽  
Zhen Wu ◽  
Xiaoqun Zeng ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Lactobacillus Acidophilus ◽  
Lactobacillus Acidophilus Ncfm

scholarly journals Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

2019 ◽  
Vol 21 (1) ◽  
pp. 91 ◽  
Author(s):  
Ly Thi Huong Luu Le ◽  
Wanki Yoo ◽  
Sangeun Jeon ◽  
Kyeong Kyu Kim ◽  
T. Doohun Kim
Keyword(s):  
Thermal Stability ◽  
Lactobacillus Acidophilus ◽  
Industrial Applications ◽  
Lactobacillus Species ◽  
Highly Active ◽  
Wide Range ◽  
Optimum Ph ◽  
Lactobacillus Acidophilus Ncfm ◽  
Glucose Pentaacetate ◽  
Naphthyl Acetate

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.

scholarly journals Rational Engineering of Hydratase from Lactobacillus acidophilus Reveals Critical Residues Directing Substrate Specificity and Regioselectivity

ChemBioChem ◽  
2019 ◽  
Vol 21 (4) ◽  
pp. 550-563 ◽  
Author(s):  
Bekir Engin Eser ◽  
Michal Poborsky ◽  
Rongrong Dai ◽  
Shigenobu Kishino ◽  
Anita Ljubic ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Lactobacillus Acidophilus ◽  
Rational Engineering ◽  
Critical Residues
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