Macrophage Stimulation Activity of the Polysaccharide Fraction from a Marine Alga (Porphyra yezoensis): Structure-Function Relationships and Improved Solubility

Yoshizawa, Yu‐ichi; Ametani, Akio; Tsunehiro, Jun; Nomura, Kazuyo; Itoh, Masao; Fukui, Fumio; Kaminogawa, Shuichi

doi:10.1271/bbb.59.1933

Cited by 158 publications

(72 citation statements)

References 7 publications

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“…Some seaweed contains high amounts of essential proteins, vitamins and minerals. Furthermore, many polysaccharides found in seaweeds have diverse biological activities, including effects on the immune system and cancer (Yashizawa et al, 1995). Yamamoto et al (1987) and Sheu et al (1996) reported that oral consumption of several seaweeds significantly decreased the incidence of carcinogenesis in vivo.…”

Section: Introductionmentioning

confidence: 99%

Antitumor activity of Chondrococcus hornemanni and Spyridia fusiformis on Dalton’s lymphoma ascites in mice

Murugesan¹,

Sundaresan²

2012

Bangladesh J Pharmacol

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Section: Introductionmentioning

confidence: 99%

Antitumor activity of Chondrococcus hornemanni and Spyridia fusiformis on Dalton’s lymphoma ascites in mice

Murugesan¹,

Sundaresan²

2012

Bangladesh J Pharmacol

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“…More frequently, ␤-agarases hydrolyze agarose yielding neoagarobiose, neoagarotetraose, or neoagarohexaose as the main products (17,(21)(22)(23). Agarases have potential applications in the food, cosmetic, and medical industries for the production of oligosaccharides from agar or agarose (24,25). Moreover, agarases can be used to degrade the cell walls of marine algae for the preparation of protoplasts and for the extraction of labile substances with biological activities (26).…”

mentioning

confidence: 99%

Molecular Cloning and Characterization of a Novel β-Agarase, AgaB, from Marine Pseudoalteromonas sp. CY24

Shi

et al. 2007

Journal of Biological Chemistry

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Agarases are generally classified into glycoside hydrolase families 16, 50, and 86 and are found to degrade agarose to frequently generate neoagarobiose, neoagarotetraose, or neoagarohexaose as the main products. In this study we have cloned a novel endo-type ␤-agarase gene, agaB, from marine Pseudoalteromonas sp. CY24. The novel agarase encoded by agaB gene has no significant sequence similarity with any known proteins including all glycoside hydrolases. It degrades agarose to generate neoagarooctaose and neoagarodecaose as the main end products. Based on the analyses of enzymatic kinetics and degradation patterns of different oligosaccharides, the agarase AgaB appears to have a large substrate binding cleft that accommodates 12 sugar units, with 8 sugar units toward the reducing end spanning subsites ؉1 to ؉8 and 4 sugar units toward the non-reducing end spanning subsites ؊4 to ؊1, and enzymatic cleavage taking place between subsites ؊1 and ؉1. In addition, 1 H NMR analysis shows that this enzyme hydrolyzes the glycosidic bond with inversion of anomeric configuration, in contrast to other known agarases that are retaining. Altogether, AgaB is structurally and functionally different from other known agarases and appears to represent a new family of glycoside hydrolase.

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“…13) Moreover, agarases can be used to degrade the cell walls of marine algae for extraction of labile substances with biological activities and for the preparation of protoplasts. 14) Most agarases that have been purified and characterized belong to the -agarase group except for anagarase from Alteromonas agarlyticus GJ1B.…”

mentioning

confidence: 99%

Enzymatic Properties and Nucleotide and Amino Acid Sequences of a Thermostable β-Agarase from the Novel Marine Isolate, JAMB-A94

Ohta¹,

Nogi²,

Miyazaki³

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Macrophage Stimulation Activity of the Polysaccharide Fraction from a Marine Alga (Porphyra yezoensis): Structure-Function Relationships and Improved Solubility

Cited by 158 publications

References 7 publications

Antitumor activity of <i>Chondrococcus hornemanni</i> and <i>Spyridia fusiformis</i> on Dalton’s lymphoma ascites in mice

Antitumor activity of <i>Chondrococcus hornemanni</i> and <i>Spyridia fusiformis</i> on Dalton’s lymphoma ascites in mice

Molecular Cloning and Characterization of a Novel β-Agarase, AgaB, from Marine Pseudoalteromonas sp. CY24

Enzymatic Properties and Nucleotide and Amino Acid Sequences of a Thermostable β-Agarase from the Novel Marine Isolate, JAMB-A94

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