Bacterial alginates: from biosynthesis to applications

被引:238
作者
Remminghorst, Uwe [1 ]
Rehm, Bernd H. A. [1 ]
机构
[1] Massey Univ, Inst Mol BioSci, Palmerston North, New Zealand
关键词
alginate; alginate polymerisation; alginate secretion; Azotobacter; biomaterial; biopolymer; guluronic acid; mannuronic acid; Pseudomonas;
D O I
10.1007/s10529-006-9156-x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Alginate is a polysaccharide belonging to the family of linear (unbranched), non-repeating copolymers, consisting of variable amounts of beta-D-mannuronic acid and its C5-epimer alpha-L-guluronic acid linked via beta-1,4-glycosidic bonds. Like DNA, alginate is a negatively charged polymer, imparting material properties ranging from viscous solutions to gel-like structures in the presence of divalent cations. Bacterial alginates are synthesized by only two bacterial genera, Pseudomonas and Azotobacter, and have been extensively studied over the last 40 years. While primarily synthesized in form of polymannuronic acid, alginate undergoes chemical modifications comprising acetylation and epimerization, which occurs during periplasmic transfer and before final export through the outer membrane. Alginate with its unique material properties and characteristics has been increasingly considered as biomaterial for medical applications. The genetic modification of alginate producing microorganisms could enable biotechnological production of new alginates with unique, tailor-made properties, suitable for medical and industrial applications.
引用
收藏
页码:1701 / 1712
页数:12
相关论文
共 73 条
[1]   A novel gene, algK, from the alginate biosynthetic cluster of Pseudomonas aeruginosa [J].
Aarons, SJ ;
Sutherland, IW ;
Chakrabarty, AM ;
Gallagher, MP .
MICROBIOLOGY-SGM, 1997, 143 :641-652
[2]   Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa [J].
Akama, H ;
Matsuura, T ;
Kashiwagi, S ;
Yoneyama, H ;
Narita, SI ;
Tsukihara, T ;
Nakagawa, A ;
Nakae, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (25) :25939-25942
[3]   Alginate lyase (AlgL) activity is required for alginate biosynthesis in Pseudomonas aeruginosa [J].
Albrecht, MT ;
Schiller, NL .
JOURNAL OF BACTERIOLOGY, 2005, 187 (11) :3869-3872
[4]   PilZ domain is part of the bacterial c-di-GMP binding protein [J].
Amikam, D ;
Galperin, MY .
BIOINFORMATICS, 2006, 22 (01) :3-6
[5]   Role of the Pseudomonas fluorescens alginate lyase (AlgL) in clearing the periplasm of alginates not exported to the extracellular environment [J].
Bakkevig, K ;
Sletta, H ;
Gimmestad, M ;
Aune, R ;
Ertesvåg, H ;
Degnes, K ;
Christensen, BE ;
Ellingsen, TE ;
Valla, S .
JOURNAL OF BACTERIOLOGY, 2005, 187 (24) :8375-8384
[6]   Construction and analyses of hybrid Azotobacter vinelandii mannuronan C-5 epimerases with new epimerization pattern characteristics [J].
Bjerkan, TM ;
Lillehov, BE ;
Strand, WI ;
Skjåk-Bræk, G ;
Valla, S ;
Ertesvåg, H .
BIOCHEMICAL JOURNAL, 2004, 381 :813-821
[7]   SEQUENCE OF THE ALGL GENE OF PSEUDOMONAS-AERUGINOSA AND PURIFICATION OF ITS ALGINATE LYASE PRODUCT [J].
BOYD, A ;
GHOSH, M ;
MAY, TB ;
SHINABARGER, D ;
KEOGH, R ;
CHAKRABARTY, AM .
GENE, 1993, 131 (01) :1-8
[8]   Characterization of the gene coding for GDP-mannose dehydrogenase (algD) from Azotobacter vinelandii [J].
Campos, ME ;
MartinezSalazar, JM ;
Lloret, L ;
Moreno, S ;
Nunez, C ;
Espin, G ;
SoberonChavez, G .
JOURNAL OF BACTERIOLOGY, 1996, 178 (07) :1793-1799
[9]   CLONING OF PSEUDOMONAS-AERUGINOSA ALGG, WHICH CONTROLS ALGINATE STRUCTURE [J].
CHITNIS, CE ;
OHMAN, DE .
JOURNAL OF BACTERIOLOGY, 1990, 172 (06) :2894-2900
[10]   GENETIC-ANALYSIS OF THE ALGINATE BIOSYNTHETIC GENE-CLUSTER OF PSEUDOMONAS-AERUGINOSA SHOWS EVIDENCE OF AN OPERONIC STRUCTURE [J].
CHITNIS, CE ;
OHMAN, DE .
MOLECULAR MICROBIOLOGY, 1993, 8 (03) :583-590