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Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer
The pattern of agarose hydrolysis showed that the enzyme was an endo-type β-agarase, and the final main product was neoagarotetraose, not inhibited by NaCl, EDTA, and various surfactants at high concentrations.
Purification and Characterization of a Novel α-Agarase from a Thalassomonas sp.
An agar-degrading Thalassomonas bacterium, strain JAMB-A33, was isolated from the sediment off Noma Point, Japan, at a depth of 230 m. A novel α-agarase from the isolate was purified to homogeneity
High-resolution quantitative imaging of mammalian and bacterial cells using stable isotope mass spectrometry
MIMS makes it possible for the first time to both image and quantify molecules labeled with stable or radioactive isotopes within subcellular compartments.
Cloning, expression, and characterization of a glycoside hydrolase family 86 β-agarase from a deep-sea Microbulbifer-like isolate
The gene for a novel β-agarase from a deep-sea Microbulbifer-like isolate was cloned and sequenced and was the first glycoside hydrolase family 86 enzyme to be homogeneously purified and characterized.
High‐level expression of a neoagarobiose‐producing β‐agarase gene from Agarivorans sp. JAMB‐A11 in Bacillus subtilis and enzymic properties of the recombinant enzyme
The structural gene for a neoagarobiose‐producing β‐agarase of an Agarivorans isolate was expressed in Bacillus subtilis. High‐level production of the recombinant enzyme was achieved corresponding to
Enzymatic Properties and Nucleotide and Amino Acid Sequences of a Thermostable β-Agarase from the Novel Marine Isolate, JAMB-A94
A gene, agaA, for a novel β-agarase from the marine bacterium JAMB-A94 was cloned and sequenced and showed 37–66% identity to those of known agarases in glycoside hydrolase family 16.
α-Glucosidase from a strain of deep-sea Geobacillus: a potential enzyme for the biosynthesis of complex carbohydrates
An α-glucosidase from Geobacillus sp. strain HTA-462, one of the deepest sea bacteria isolated from the sediment of the Mariana Trench, was purified to homogeneity and estimated to be a 65-kDa
Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme.
The crystal structure of the catalytic domain of alkaline cellulase K was determined and a mechanism similar to that previously proposed for alkaline proteases was suggested, which appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.
Novel α-Amylase That Is Highly Resistant to Chelating Reagents and Chemical Oxidants from the AlkaliphilicBacillus Isolate KSM-K38
A novel α-amylase (AmyK38) was found in cultures of an alkaliphilic Bacillus isolate designated KSM-K38 and maintained more than 80% of its original activity even after incubation for 1 h in the presence of excess H2O2.
New microbial mannan catabolic pathway that involves a novel mannosylglucose phosphorylase.
A new mannan catabolic pathway in the anaerobe is proposed, which involves 1,4-β-mannanase, a mannobiose and/or sugar transporter, and mannosylglucose phosphorylase, finally progressing to glycolysis.