Microwave assisted rapid method for hydrolysis of sodium alginate for M/G ratio determination

Chhatbar, Mahesh U.; Meena, Ramavatar; Prasad, Kamalesh; Siddhanta, A. K.

doi:10.1016/j.carbpol.2008.11.033

Cited by 54 publications

(24 citation statements)

References 16 publications

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“…However, no spots were found for sodium alginate and polyG (data not shown). Chemical shifts for the 13 C NMR spectra obtained for the sodium alginate (dNaOH) were δ=100.69 depolymerized polyG (δ=101.11, 99.62, 66.61, 70.27, 71.43, 76.75, 75.62, 67.0, 86.10, 175.12) and polyM (δ=99.77, 99.68, 69.79, 66.96, 71.43, 70.25, 79.09, 76.83, 75.56, 175.24) were found to be comparable with the report of Chhatbar et al (2009).…”

Section: Viscometric Assay Ft-ir Nmr Spectroscopy and Tlcsupporting

confidence: 92%

“…Comparison of chemical shift in the 13 C NMR spectra of both polyM and polyG with that of sodium alginate shows evidence for depolymerization of the substrate. The 13 C NMR spectra and FT-IR findings of enzymatically depolymerized sodium alginate support the fact that the alginate lyase obtained in the present study has got specificity for cleaving the polymer at the β-1,4 glycosidic link (Chhatbar et al 2009). …”

Section: Discussionsupporting

confidence: 77%

“…In contrast, acid hydrolysis results in random cleavage along the polysaccharide chain, producing polysaccharide fragments with unmodified hexuronic acid residues at both ends. Most recently, Chhatbar et al (2009) reported a rapid microwave-assisted acid hydrolysis of alginate giving rise to corresponding oligosaccharide fragments as final products.…”

Section: Introductionmentioning

confidence: 99%

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Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

et al. 2010

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The extracellular enzyme alginate lyase produced from marine fungus Aspergillus oryzae isolated from brown alga Dictyota dichotoma was purified, partially characterized, and evaluated for its sodium alginate depolymerization abilities. The enzyme characterization studies have revealed that alginate lyase consisted of two polypeptides with about 45 and 50 kDa each on 10% sodium dodecyl sulfate polyacrylamide gel electrophoresis and showed 140-fold higher activity than crude enzyme under optimized pH (6.5) and temperature (35°C) conditions. Zn 2+ , Mn 2+ , Cu 2+ , Mg 2+ , Co 2+ and NaCl were found to enhance the enzyme activity while (Ca 2+ , Cd 2+ , Fe 2+ , Hg 2+ , Sr 2+ , Ni 2+ ), glutathione, and metal chelators (ethylenediaminetetraacetic acid and ethylene glycol tetraacetic acid) suppressed the activity. Fourier transform infrared and thin-layer chromatography analysis of depolymerized sodium alginate indicated the enzyme specificity for cleaving at the β-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate and therefore resulted in estimation of relatively higher polyM content than polyG. Comparison of chemical shifts in 13 C nuclear magnetic resonance spectra of both polyM and polyG from that of sodium alginate also showed further evidence for enzymatic depolymerization of sodium alginate.

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Section: Viscometric Assay Ft-ir Nmr Spectroscopy and Tlcsupporting

confidence: 92%

Section: Discussionsupporting

confidence: 77%

Section: Introductionmentioning

confidence: 99%

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Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

et al. 2010

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“…Enriched polyG and polyM were produced using the method of Chhatbar and coworkers (44). Briefly, 4 g of sodium alginate dissolved in 0.25 M H 2 SO 4 was microwaved for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Alginate Lyases from Alginate-Degrading Vibrio splendidus 12B01 Are Endolytic

Badur

Jagtap

Yalamanchili

et al. 2015

Appl Environ Microbiol

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bAlginate lyases are enzymes that degrade alginate through ␤-elimination of the glycosidic bond into smaller oligomers. We investigated the alginate lyases from Vibrio splendidus 12B01, a marine bacterioplankton species that can grow on alginate as its sole carbon source. We identified, purified, and characterized four polysaccharide lyase family 7 alginates lyases, AlyA, AlyB, AlyD, and AlyE, from V. splendidus 12B01. The four lyases were found to have optimal activity between pH 7.5 and 8.5 and at 20 to 25°C, consistent with their use in a marine environment. AlyA, AlyB, AlyD, and AlyE were found to exhibit a turnover number (k cat ) for alginate of 0.60 ؎ 0.02 s ؊1 , 3.7 ؎ 0.3 s ؊1 , 4.5 ؎ 0.5 s ؊1 , and 7.1 ؎ 0.2 s ؊1 , respectively. The K m values of AlyA, AlyB, AlyD, and AlyE toward alginate were 36 ؎ 7 M, 22 ؎ 5 M, 60 ؎ 2 M, and 123 ؎ 6 M, respectively. AlyA and AlyB were found principally to cleave the ␤-1,4 bonds between ␤-D-mannuronate and ␣-L-guluronate and subunits; AlyD and AlyE were found to principally cleave the ␣-1,4 bonds involving ␣-L-guluronate subunits. The four alginate lyases degrade alginate into longer chains of oligomers. Alginate is an abundant polysaccharide found within the cell wall of brown seaweeds (1) and comprises approximately 40% of the dry weight of the plant (2). Alginate is a copolymer consisting of the 1,4-linked epimers ␣-L-guluronate (G) and ␤-Dmannuronate (M). The individual monomeric subunits are organized in short stretches of polyguluronate (polyG), polymannuronate (polyM), or alternating sequences of mannuronate and guluronate (polyMG) (3). Alginate recently has been considered as a source for bioenergy, as it offers several potential advantages over terrestrial biomass. In particular, the farming of algae does not impinge on arable land; hence, it avoids the conflict between food and energy (4, 5). Algae also display higher growth rates than terrestrial plants (6). Finally, algae lack crystalline cellulose and lignin (7,8), bypassing a key obstacle to biofuel production.Alginate lyases are enzymes that degrade alginate through the ␤-elimination of the glycosidic bond into smaller oligomers. These enzymes can be classified based on the specific dyad G-G (EC 4.2.2.11) (9, 10), M-M (EC 4.2.2.3) (11), and M-G/G-M (12) bonds that they cleave. Additionally, alginate lyases can have either endocleaving or exocleaving specificity, with the majority of alginate lyases having an endocleaving preference (3). Along with the substrate specificity, alginate lyases also are characterized by their structure, termed polysaccharide lyase (PL) families. A total of seven PL families have been identified: PL5, PL6, PL7, PL14, PL15, PL17, and PL18 (13, 14). The most prevalent of these families is PL7 (Carbohydrate Active Enzymes database; http://www .cazy.org). The PL7 domain contains a ␤-jelly roll that consists of ␤-sheets in an antiparallel, adjacent barrel forming a cleft (12). This cleft contains three adjacent ␤-sheets that contain the catalytic residues (15). PL7 contains enzymes...

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“…The precipitate was dried over night at 70 • C. The dried sample was taken to FTIR and NMR analyses. After the acid hydrolysis, poly(mannuronic acid), PMA, and poly(guluronic acid), PGA, were isolated from the hydrolyzed sample using a pH dependent method (Chandía, Matsuhiro, & Vásquez, 2001;Chhatbar, Meena, Prasad, & Siddhanta, 2009). The hydrolyzed products were dissolved in 0.1 M Na 2 CO 3 .…”

Section: Analysis Of Polymer Components In Sodium Alginatementioning

confidence: 99%

Encapsulated eucalyptus oil in ionically cross-linked alginate microcapsules and its controlled release

Noppakundilograt

Piboon

Graisuwan

et al. 2015

Carbohydrate Polymers

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Microwave assisted rapid method for hydrolysis of sodium alginate for M/G ratio determination

Cited by 54 publications

References 16 publications

Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

Alginate Lyases from Alginate-Degrading Vibrio splendidus 12B01 Are Endolytic

Encapsulated eucalyptus oil in ionically cross-linked alginate microcapsules and its controlled release

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