2015
DOI: 10.1007/s00253-015-6983-5
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Biochemical and genetic characterization of β-1,3 glucanase from a deep subseafloor Laceyella putida

Abstract: A β-1,3-glucanase (LpGluA) of deep subseafloor Laceyella putida JAM FM3001 was purified to homogeneity from culture broth. The molecular mass of the enzyme was around 36 kDa as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). LpGluA hydrolyzed curdlan optimally at pH 4.2 and 80 °C. In spite of the high optimum temperature, LpGluA showed relatively low thermostability, which was stabilized by adding laminarin, xylan, colloidal chitin, pectin, and its related polysaccharides. The g… Show more

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Cited by 16 publications
(10 citation statements)
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“…When the enzyme reactions were conducted in the presence of tryptophan (Trp) residue-specific modifiers including Hg 2+ (1 mM) and N-bromosuccinimide (5 mM), rGluY was considerably inactivated by the compounds (Figure 4). Previously, a similar observation was also made with a GH64 endo-β-1,3-glucanase from S. matensis DIC-108 [6] reacted with curdlan in the presence of Hg 2+ (>20 µM), although the biocatalytic activity of Laceyella putida GH16 endo-β-1,3-glucanase [27] was only moderately suppressed by the metal ion. Taken together, the findings were consistent with the fact that N-bromosuccinimide and Hg 2+ ions oxidize the indole ring of strictly conserved Trp residues in the active site of endotype GH enzymes, which essentially participate in enzyme-substrate interaction [28,29].…”
Section: Biocatalytic Characterization Of Recombinant Enzymessupporting
confidence: 70%
“…When the enzyme reactions were conducted in the presence of tryptophan (Trp) residue-specific modifiers including Hg 2+ (1 mM) and N-bromosuccinimide (5 mM), rGluY was considerably inactivated by the compounds (Figure 4). Previously, a similar observation was also made with a GH64 endo-β-1,3-glucanase from S. matensis DIC-108 [6] reacted with curdlan in the presence of Hg 2+ (>20 µM), although the biocatalytic activity of Laceyella putida GH16 endo-β-1,3-glucanase [27] was only moderately suppressed by the metal ion. Taken together, the findings were consistent with the fact that N-bromosuccinimide and Hg 2+ ions oxidize the indole ring of strictly conserved Trp residues in the active site of endotype GH enzymes, which essentially participate in enzyme-substrate interaction [28,29].…”
Section: Biocatalytic Characterization Of Recombinant Enzymessupporting
confidence: 70%
“…The glycoside hydrolase β-1,3-glucanase, extensively distributed among plants, fungi, and bacteria, acts on 1,3-β-glucosidic bonds of structural β-1,3-glucans to hydrolyze or transfer glycosides [ 1 , 2 ]. Based on the hydrolysis position, β-1,3-glucanases are divided into endo-type (E.C.…”
Section: Introductionmentioning
confidence: 99%
“…Elisitor β-1,3-glukan dapat dihasilkan oleh aktivitas β-1,3-glukanase, baik yang berasal dari tanaman (Mishra et al 2012) maupun mikroba endofitik (Shoresh et al 2010;Chen et al 2016). Induksi elisitor β-1,3-glukan terbukti meningkatkan ketahanan tanaman terhadap virus, bakteri, dan jamur patogen, seperti pada tanaman Arabidopsis (Ménard et al 2004), padi (Inui et al 1997), alfalfa (Kobayashi et al 2016), anggur (Aziz et al 2003, dan kedelai (Fliegmann et al 2004). Tanaman kedelai yang diinduksi dengan elisitor β-1,3-glukan dari P. sojae f.sp.…”
Section: Pendahuluanunclassified