The thermophilic bacteria hydrolyzing agar: Characterization of thermostable agarase

Bannikova, G. E.; Лопатин, С. А.; Варламов, В. П.; Кузнецов, Б. Б.; Kozina, Irina V.; Miroshnichenko, M. L.; Chernykh, N. A.; Turova, T P; Bonch-Osmolovskaya, E. A.

doi:10.1134/s0003683808040054

Cited by 17 publications

(15 citation statements)

References 25 publications

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“…concentration, the catalytic activity and thermostability of both the wild-type and mutant b-agarases could be enhanced. Shieh and Jean (1998) reported on a thermophilic agarase of Alterococcus agarolyticus, and Bannikova et al (2008) reported on thermostable agarase of Caldoanaerobacter and Thermoanaerobacter species. However, these bacteria are anaerobes and the enzymes have not yet been cloned and well characterized.…”

Section: Discussionmentioning

confidence: 98%

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Enhancement of the thermostability of a recombinant β-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis

Jang

Lee

et al. 2010

Biotechnol Lett

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Random mutagenesis was performed on beta-agarase, AgaB, from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutants E99K, T307I and E99K-T307I were approx. 140, 190 and 200%, respectively, of wild type beta-agarase (661 U/mg) at 40 degrees C. All three mutant enzymes were stable up to 50 degrees C and E99K-T307I had the highest thermostability. The melting temperature (Tm) of E99K-T307I, determined by CD spectra, was increased by 5.2 degrees C over that of the wild-type enzyme (54.6 degrees C). Activities of both the wild-type and E99K-T307I enzymes, as well as their overall thermostabilities, increased in 1 mM CaCl2. The E99K-T307I enzyme was stable at 55 degrees C with 1 mM CaCl2, reaching 260% of the activity the wild-type enzyme held at 40 degrees C without CaCl2.

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Section: Discussionmentioning

confidence: 98%

“…Alterococcus agarolyticus (Shieh and Jean 1998), Thermoanaerobater and Caldoanaerobacter sp. (Bannikova et al 2008) were reported to have agarolytic activity and optimum growth over 50°C. However, mass production of agarase was not reported, which may be due to their anaerobic/slow growth or difficulties with cloning the agarase gene.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of the thermostability of a recombinant β-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis

Jang

Lee

et al. 2010

Biotechnol Lett

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“…Agarose is a linear polymer of alternating units of 3-O-bound β-D-galactopyranosides and 4-O-bound 3,6-anhydro-α-galactopyranoses, whereas agaropectin has an intricate yet vague structure. There are only a few organisms capable of hydrolyzing agar, which allows agar to be widely used as a gelling agent for microbiological media [4].…”

Section: Introductionmentioning

confidence: 99%

“…Based on the sites of hydrolysis, agarases are characterized as α-agarases and β-agarases. The α-agarases cleave the α-L- (1,3) linkages of agarose to produce oligosaccharides of the agarobiose series with 3,6anhydro-L-galactopyranose at the reducing end, whereas the β-agarases cleave the β-D- (1,4) linkages of agarose to produce neoagarooligosaccharides with D-galactopyranoside residues at the reducing end [28]. Agarases can be used to prepare protoplasts and extract biological substances, such as unsaturated fatty acids, vitamins, carotenoids, betaine, among others, from algae [3].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Thermostable Agarase from Bacillus sp. BI-3, a Thermophilic Bacterium Isolated from Hot Spring

Li¹,

Sha²,

Zilda³

et al. 2014

Journal of Microbiology and Biotechnology

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An extracellular agarase was purified from Bacillus sp. BI-3, a thermophilic agar-degrading bacterium isolated from a hot spring in Indonesia. The purified agarase revealed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with an apparent molecular mass of 58 kDa. The optimum pH and temperature of the agarase were 6.4 and 70°C, respectively. The activity of the agarase was stable at high temperatures, and more than 50% activity was retained at 80°C for 15 min. Furthermore, the enzyme was stable in the pH range of 5.8-8.0, and more than 60% of the residual activity was retained. Significant activation of the agarase was observed in the presence of K(+), Na(+), Ca(2+), Mg(2+), and Sr(2+); on the other hand, Ba(2+), Zn(2+), Cu(2+), Mn(2+), Co(2+), Fe(2+), and EDTA inhibited or inactivated the enzyme activity. The components of the hydrolytic product analyzed by thin-layer chromatography showed that the agarase mainly produced neoagarobiose. This study is the first to present evidence of agarolytic activity in aerobic thermophilic bacteria.

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“…한천분해산물의 기능성 한천과 같은 황함유 다당류와 한천 분해산물은 항응고 작 [116], Alteromonas [68,99,111], Aquimarina [83], Coraliomargarita [88], Cytophaga [22,136], Flammeovirga [143], Glaciecola [78,145], Microbulbifer [65,106,107], Microscilla [152], Pseudoalteromonas [85,86,101,102,115] Pseudomonas [6,10,61,94], Pseudozobellia [96], Saccharophagus [26,36,67,117,148], Simiduia [64], Thalassomonas [77,103], Thermoanaerobacter [9], Vibrio [150], Zobellia [55,79] 등이며, 비 해양유래 세균의 속으로는 Acinetobacter [74], Asticcacaulis [44], Bacillus [52], Caldoanaerobacter [9], Cellvibrio [112], Cytophaga [138], Alteromonas [1], Cellulophaga [59], Paenibacillus [132], Spirochaeta [151], Streptomyces …”

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The Classification, Origin, Collection, Determination of Activity, Purification, Production, and Application of Agarases

Lee¹,

Lee

2012

Journal of Life Science

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Agar is a cell wall component of macro red algae that can be hydrolyzed by agarase. Agarases are classified into α-agarase (E.C. 3.2.1.158) and β-agarase (E.C. 3.2.1.81), in accordance with their cleavage pattern, and can be grouped in the glycoside hydrolase (GH)-16, -58, -86, -96, and -118 family according to the amino acid sequences of the proteins. Many agarases and/or their genes have been detected, isolated, and recombinantly expressed from bacteria, and metagenomes have their origins in sea and terrestrial environments. Products of agarases, agarooligosaccharides and neoagarooligosaccharides, represent wide functions such as antitumor, immune stimulation, antioxidation, prebiotic, hepa-protective, antibacterial, whitening, and moisturizing effects; hence, broad applications would be possible in the food industry, cosmetics, and medical fields. In addition, agarases are also used as a tool enzyme for research. This paper reviews the sources, purifications and detection methods, and application fields of agarases. The role of agarases in agar metabolism and the function of their enzymatic products are also surveyed.

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The thermophilic bacteria hydrolyzing agar: Characterization of thermostable agarase

Cited by 17 publications

References 25 publications

Enhancement of the thermostability of a recombinant β-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis

Enhancement of the thermostability of a recombinant β-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis

Purification and Characterization of Thermostable Agarase from Bacillus sp. BI-3, a Thermophilic Bacterium Isolated from Hot Spring

The Classification, Origin, Collection, Determination of Activity, Purification, Production, and Application of Agarases

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