scholarly journals Recombinant Expression and Characterization of a Reducing-End Xylose-Releasing Exo-Oligoxylanase from Bifidobacterium adolescentis

2007 ◽  
Vol 73 (16) ◽  
pp. 5374-5377 ◽  
Author(s):  
Stijn Lagaert ◽  
Steven Van Campenhout ◽  
Annick Pollet ◽  
Tine M. Bourgois ◽  
Jan A. Delcour ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Glycoside Hydrolase ◽  
Recombinant Expression ◽  
Recombinant Enzyme ◽  
Bifidobacterium Adolescentis ◽  
New Class ◽  
The Family

ABSTRACT The family 8 glycoside hydrolase (RexA) from Bifidobacterium adolescentis was expressed in Escherichia coli. The recombinant enzyme was characterized as a reducing-end xylose-releasing exo-oligoxylanase. Apart from giving insights into this new class of enzymes, knowledge of the RexA enzyme helps to postulate a mechanism for the B. adolescentis breakdown of prebiotic xylooligosaccharides.

scholarly journals Characterization of Fusarium oxysporum β-1,6-Galactanase, an Enzyme That Hydrolyzes Larch Wood Arabinogalactan

2007 ◽  
Vol 73 (9) ◽  
pp. 3109-3112 ◽  
Author(s):  
Tatsuji Sakamoto ◽  
Yuya Taniguchi ◽  
Shiho Suzuki ◽  
Hideshi Ihara ◽  
Haruhiko Kawasaki
Keyword(s):  
Fusarium Oxysporum ◽  
Glycoside Hydrolase ◽  
Recombinant Enzyme ◽  
Glycoside Hydrolase Family ◽  
Type Ii ◽  
High Similarity ◽  
Degrading Enzyme ◽  
Larch Wood ◽  
Hydrolase Family

ABSTRACT A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a β-1,6-galactanase that preferentially debranches β-1,6-galactobiose from the substrate.

scholarly journals Characterization of an Alkaline GH49 Dextranase from Marine Bacterium Arthrobacter oxydans KQ11 and Its Application in the Preparation of Isomalto-Oligosaccharide

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 479 ◽  
Author(s):  
Hongfei Liu ◽  
Wei Ren ◽  
Mingsheng Ly ◽  
Haifeng Li ◽  
Shujun Wang
Keyword(s):  
Escherichia Coli ◽  
Marine Bacteria ◽  
Recombinant Expression ◽  
Bifidobacterium Longum ◽  
Lactobacillus Rhamnosus ◽  
Km Value ◽  
Tlc Analysis ◽  
Layer Chromatography ◽  
Arthrobacter Oxydans

A GH49 dextranase gene DexKQ was cloned from marine bacteria Arthrobacter oxydans KQ11. It was recombinantly expressed using an Escherichia coli system. Recombinant DexKQ dextranase of 66 kDa exhibited the highest catalytic activity at pH 9.0 and 55 °C. kcat/Km of recombinant DexKQ at the optimum condition reached 3.03 s−1 μM−1, which was six times that of commercial dextranase (0.5 s−1 μM−1). DexKQ possessed a Km value of 67.99 µM against dextran T70 substrate with 70 kDa molecular weight. Thin-layer chromatography (TLC) analysis showed that main hydrolysis end products were isomalto-oligosaccharide (IMO) including isomaltotetraose, isomaltopantose, and isomaltohexaose. When compared with glucose, IMO could significantly improve growth of Bifidobacterium longum and Lactobacillus rhamnosus and inhibit growth of Escherichia coli and Staphylococcus aureus. This is the first report of dextranase from marine bacteria concerning recombinant expression and application in isomalto-oligosaccharide preparation.

Recombinant expression, purification and characterization of antimicrobial peptide ORBK in Escherichia coli

2014 ◽  
Vol 95 ◽  
pp. 182-187 ◽  
Author(s):  
Yan Li ◽  
Jiarong Wang ◽  
Jing Yang ◽  
Chanjuan Wan ◽  
Xiaoming Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Peptide ◽  
Recombinant Expression ◽  
Purification And Characterization

scholarly journals Identification and Characterization of an Archaeon-Specific Riboflavin Kinase

2008 ◽  
Vol 190 (7) ◽  
pp. 2615-2618 ◽  
Author(s):  
Zahra Mashhadi ◽  
Hong Zhang ◽  
Huimin Xu ◽  
Robert H. White
Keyword(s):  
Escherichia Coli ◽  
Metal Ion ◽  
Biosynthetic Pathway ◽  
Recombinant Expression ◽  
Cell Extract ◽  
Flavin Mononucleotide ◽  
E Coli ◽  
Gene Recombinant ◽  
Identification And Characterization

ABSTRACT The riboflavin kinase in Methanocaldococcus jannaschii has been identified as the product of the MJ0056 gene. Recombinant expression of the MJ0056 gene in Escherichia coli led to a large increase in the amount of flavin mononucleotide (FMN) in the E. coli cell extract. The unexpected features of the purified recombinant enzyme were its use of CTP as the phosphoryl donor and the absence of a requirement for added metal ion to catalyze the formation of FMN. Identification of this riboflavin kinase fills another gap in the archaeal flavin biosynthetic pathway. Some divalent metals were found to be potent inhibitors of the reaction. The enzyme represents a unique CTP-dependent family of kinases.

Identification of a halophilic α-amylase gene from Escherichia coli JM109 and characterization of the recombinant enzyme

2013 ◽  
Vol 35 (7) ◽  
pp. 1061-1065 ◽  
Author(s):  
Yutuo Wei ◽  
Xiaobo Wang ◽  
Jiayuan Liang ◽  
Xue Li ◽  
Liqin Du ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Enzyme ◽  
Amylase Gene ◽  
Escherichia Coli Jm109

Expression of the pyranose 2-oxidase from Trametes pubescens in Escherichia coli and characterization of the recombinant enzyme

2005 ◽  
Vol 120 (4) ◽  
pp. 387-395 ◽  
Author(s):  
Helena Marešová ◽  
Branislav Večerek ◽  
Marcela Hradská ◽  
Nathalie Libessart ◽  
Stanislav Bečka ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Enzyme
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