Results 211 to 220 of about 111,667 (274)

Bacterial alginate lyase gene: Nucleotide sequence and molecular route for generation of alginate lyase species

Journal of Fermentation and Bioengineering, 1993
Abstract A bacterium (strain A1) isolated from a ditch synthesized three types of intracellular alginate lyases: A1-I (molecular weight [M.W.] 60,000), A1-II-2 (M.W. 25,000) and A1-III (M.W. 38,000). The nucleotide sequence of the gene for A1-I lyase, which has been cloned in Escherichia coli DH1 was determined.
Kousaku Murata, Tomohiro Hisano, Tetsuo Yamashita, Akira Kimura, Shiro Abe, Kenji Sakaguchi, Yoshimasa Yonemoto, Hirokazu Tanaka   +7 more
openaire   +2 more sources

Overexpression of alginate lyase of Pseudoalteromonas elyakovii in Escherichia coli, purification, and characterization of the recombinant alginate lyase

World Journal of Microbiology and Biotechnology, 2007
The alyPEEC gene encoding alginate lyase from marine bacterium Pseudoalteromonas elyakovii IAM 14594 was subcloned into pBAD24 with arabinose promoter and sequenced, and overexpressed in TOP10 strain of E. coli after arabinose induction. Expression levels of alyPEEC gene in E. coli cells were over 39.6-fold higher than those in P.
Zhen-Ming Chi, Jing Li, Liang Wu, L. Y. Ma   +3 more
openaire   +2 more sources

Alginate lyase: Structure, property, and application

Biotechnology and Bioprocess Engineering, 2011
Alginate is a linear polysaccharide in which β-D-mannuronate (M) and its epimer, α-L-guluronate (G), are covalently (1–4)-linked in different sequences. Alginate is mainly used as a food additive to modify food texture due to its high viscosity and gelling property.
Hee Sook Kim, Eun Yeol Lee, Choul-Gyun Lee   +2 more
openaire   +2 more sources

Computer-Aided Rational Design Strategy to Improve the Thermal Stability of Alginate Lyase AlyMc.

Journal of Agricultural and Food Chemistry
Alginate lyase degrades alginate by the β-elimination mechanism to produce unsaturated alginate oligosaccharides (UAOS), which have better bioactivities than saturated AOS.
Yongyan Cui, Min Yang, Nan Liu, Shanshan Wang, Yong Sun, Guohui Sun, H. Mou, Deqing Zhou   +7 more
semanticscholar   +1 more source

On the self-processing of bacterial alginate lyase

Journal of Fermentation and Bioengineering, 1994
Abstract All of the alginate lyase species (A1-I, A1-II and A1-III) in a bacterium (strain A1) isolated from a ditch are generated from a common precursor protein (A1-0) having a molecular size of 69 kDa (Murata et al., J. Ferment. Bioeng., 76, 427–437, 1993).
Tetsuo Yamashita, Kousaku Murata, Minoru Nishimura, Tomohiro Hisano, Kenji Sakaguchi   +4 more
openaire   +2 more sources

Action Pattern of a Novel G-Specific Alginate Lyase: Determination of Subsite Specificity by HPAEC-PAD/MS.

Journal of Agricultural and Food Chemistry, 2023
G-specific alginate lyases are important tools for alginate fragment biodegradation and oligosaccharide production, which have great potential in alginate refining research. In this research, a novel G-specific alginate lyase Aly7Ce was cloned, expressed,
Jiajing Li, Changhu Xue, Jingjing Shen, Guanchen Liu, Xuanwei Mei, Menghui Sun, Yaoguang Chang   +6 more
semanticscholar   +1 more source

A Novel Bifunctional Alginate Lyase and Antioxidant Activity of the Enzymatic Hydrolysates.

Journal of Agricultural and Food Chemistry
Alginate lyase Aly448, a potential new member of the polysaccharide lyase (PL) 7 family, which was cloned and identified from the macroalgae-associated bacterial metagenomic library, showed bifunctionality.
xiaoqian gu, Li-Zhong Fu, Zhiyan Wang, Zhe Cao, Luying Zhao, Dewi Seswita-Zilda, Ao Zhang, Qian Zhang, Jiang Li   +8 more
semanticscholar   +1 more source

Characterization of Alginate Lyase Activity on Liquid, Gelled, and Complexed States of Alginate

Biotechnology Progress, 2007
A study of alginate lyase was carried out to determine if this enzyme could be used to remove alginate present in the core of alginate/poly-L-lysine (AG/PLL) microcapsules in order to maximize cell growth and colonization. A complete kinetic study was undertaken, which indicated an optimal activity of the enzyme at pH 7-8, 50 degrees C, in the presence
Veronique Breguet, Urs von Stockar, Ian W. Marison   +2 more
openaire   +3 more sources

Bacterial alginate lyase inactive on alginate biosynthesized by Pseudomonas aeruginosa

Journal of Fermentation and Bioengineering, 1993
A bacterium (strain Al) isolated from a ditch produces three kinds of intracellular alginate lyases [Al-I (molecular weight: M.W. 60,000), Al-II-1 (M.W. 60,000) and Al-II-2]; the former two lyases have been purified and characterized (Yonemoto et al., J. Ferment. Bioeng., 72, 152–157, 1991).
Kousaku Murata, Tetsuo Yamashita, Tomohiro Hisano, Kenji Sakaguchi, Shiro Abe, Yoshimasa Yonemoto, Akira Kimura, Hisako Yamaguchi   +7 more
openaire   +2 more sources

Elucidation of degradation pattern and immobilization of a novel alginate lyase for preparation of alginate oligosaccharides

International Journal of Biological Macromolecules, 2020
Alginate lyases are important enzymes to prepare alginate oligosaccharides for industrial applications and elucidating the degradation pattern of alginate lyases is essential for expanding their applications. Herein, we cloned and expressed AlyPL6, a novel member of polysaccharide lyase family-6 (PL6) with high activity from Pedobacter hainanensis NJ ...
Benwei Zhu, Fu Hu, Qian Li, Mingyang Wang, Fang Ni, Zhong Yao   +5 more
openaire   +3 more sources