Results 201 to 210 of about 8,032 (242)

Bacterial alginate lyase highly active on acetylated alginates

Journal of Fermentation and Bioengineering, 1993
Abstract A bacterium (strain A1) isolated from a ditch synthesized three kinds of intracellular alginate lyases: A1-I (molecular weight [M.W.] 60,000), A1-II-1 (M.W. 60,000) and A1-II-2 (M.W. 25,000) in laboratory-scale cultures. However, when cells of strain A1 were grown on an industrial scale, another lyase (A1-III) was produced other than A1-I ...
Tomohiro Hisano, Minoru Nishimura, Yoshimasa Yonemoto, Shiro Abe, Tetsuo Yamashita, Kenji Sakaguchi, Akira Kimura, Kousaku Murata   +7 more
  +4 more sources

Bacterial alginate lyase: Characterization of alginate lyase-producing bacteria and purification of the enzyme

Journal of Fermentation and Bioengineering, 1991
Abstract Two kinds of bacteria producing alginate lyase were isolated from ditch sample and they were designated A-1 and A-2 strains. Morphological and physiological properties of the two strains were closely similar to each other, except that the cells of strain A-1 showed flocculation during growth on a medium containing alginate as a carbon source.
Yoshimasa Yonemoto, Kousaku Murata, Akira Kimura, Hisako Yamaguchi, Kenichi Okayama   +4 more
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Characteristics and applications of alginate lyases: A review

International Journal of Biological Macromolecules, 2020
Brown algae, as the main source of alginate, are a type of marine biomass with a very high output. Alginate, a polysaccharide composed of β-D-mannuronic acid (M) and α-L-guluronic acid (G), has great potential for applications in the food, cosmetic and pharmaceutical industries. Alginate lyases (Alys) can degrade alginate polymers into oligosaccharides
Danyang, Cheng, Chengcheng, Jiang, Jiachao, Xu, Zhen, Liu, Xiangzhao, Mao   +4 more
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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).
Tomohiro Hisano, Hisako Yamaguchi, Yoshimasa Yonemoto, Kenji Sakaguchi, Tetsuo Yamashita, Shiro Abe, Akira Kimura, Kousaku Murata   +7 more
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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, Choul-Gyun Lee, Eun Yeol Lee   +2 more
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Kinetics and specificity of alginate lyases

Hydrobiologia, 1993
A purified preparation of the extracellular alginate lyase has been used to study kinetics and specificity towards purified, homopolymeric fragments of alginate. The enzyme preparation from Bacillus circulans 1351 degraded both block types, although with different efficiency, and thus appears to be nonspecific.
Bj�rn Larsen, Kirsti Ho�en, Kjetill �stgaard   +2 more
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Alginate production by an Azotobacter vinelandii mutant unable to produce alginate lyase

Applied Microbiology and Biotechnology, 2003
Alginate is an industrially relevant linear copolymer composed of beta-1,4-linked D-mannuronic acid and its C-5 epimer L-guluronic acid. The rheological and gel-forming properties of alginates depend on the molecular weight and the relative content of the two monomers. Alginate produced by Azotobacter vinelandii was shown to be degraded towards the end
M A, Trujillo-Roldán, S, Moreno, D, Segura, E, Galindo, G, Espín   +4 more
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Preparation of Dye-labeled Alginate for the Assay of Alginate Lyase

Bioscience, Biotechnology, and Biochemistry, 1997
Dabsyl-alginate, the dye-labeled substrate of alginate lyase, was prepared. Low-viscosity alginate, which was prepared by enzymatic degradation of sodium alginate, and tetramethylenediamine were conjugated by reductive amination. Then, dabsyl-Cl was coupled with the primary amino group of the aminobutyl-alginate. The assay for endo-alginate lyase using
Shigeki Yoshida, Sayaka Watanabe, Toshio Takeuchi, Katsumi Murata, Isao Kusakabe   +4 more
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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
Véronique, Breguet, Urs, von Stockar, Ian W, Marison   +2 more
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Degradable alginate hydrogel microfiber for cell-encapsulation based on alginate lyase loaded nanoparticles

Materials Today Communications, 2021
Abstract Cell-encapsulation in hydrogels is a promising strategy for tissue engineering and cell therapy, particularly alginate hydrogels as they immobilize the cells in porous matrices, which allows an exchange of nutrients and oxygen and protects the cells from immune clearance.
Wisawat Keaswejjareansuk, Somrudee Keawmaloon, Nuttawat Sawangrat, Satit Puttipipatkhachorn, Teerapong Yata, Phornphimon Maitarad, Liyi Shi, Mattaka Khongkow, Katawut Namdee   +8 more
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