Kinetic Analysis of a Chitinase from Red Sea Bream,<i>Pagrus major</i>

Karasuda, Shuji; Yamamoto, Kosuke; Kono, Michiko; Sakuda, Shohei; Koga, Daizo

doi:10.1271/bbb.68.1338

Cited by 17 publications

(9 citation statements)

References 27 publications

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“…Thus, it is very likely that HoChiA, HoChiB, HoChiC, and SjChi all belong to family 18 glycosyl hydrolases, as does Pagrus major chitinase. 27) This hypothesis is strongly supported by our cloning data for the cDNAs from HoChiA, HoChiB, HoChiC, and SjChi encoding the region between the N-terminus and conserved region II of family 18 chitinases (unpublished data). These cDNA fragments have both conserved regions I and II of family 18 chitinases and the catalytically critical residues, DWE (-Asp-Trp-Glu-) within conserved region II.…”

Section: Discussionmentioning

confidence: 53%

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Substrate Specificity of Chitinases from Two Species of Fish, Greenling,Hexagrammos otakii, and Common Mackerel,Scomber japonicus, and the Insect, Tobacco Hornworm,Manduca sexta

Matsumiya

Arakane

Haga

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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Three chitinase isozymes, HoChiA, HoChiB, and HoChiC, were purified from the stomach of the greenling, Hexagrammos otakii, by ammonium sulfate fractionation, followed by column chromatography on Chitopearl Basic BL-03 and CM-Toyopearl 650S. The molecular masses and pIs of HoChiA, HoChiB, and HoChiC are 62 kDa and pH 5.7, 51 kDa and pH 7.6, and 47 kDa and pH 8.8, respectively. Substrate specificities of these chitinases were compared with those of another fish stomach chitinase from the common mackerel, Scomber japonicus (SjChi), as well as two from the tobacco hornworm, Manduca sexta (MsChi535 and MsChi386). The efficiency parameters, kcat/Km, toward glycolchitin for HoChiA and SjChi were larger than those for HoChiB and HoChiC. The relative activities of HoChiA and SjChi toward various forms of chitin were as follows: shrimp shell or crab shell alpha-chitin > beta-chitin >> silkworm cuticle alpha-chitin. On the other hand, the relative activities of HoChiB and HoChiC were beta-chitin >> silkworm alpha-chitin > shrimp and crab alpha-chitin. MsChi535 preferred silkworm alpha-chitin to shrimp and crab alpha-chitins, and no activity was observed toward beta-chitin. MsChi386, which lacked the C-terminal linker region and the chitin-binding domain, did not hydrolyze silkworm alpha-chitin. These results demonstrate that fish and insect chitinases possess unique substrate specificities that are correlated with their physiological roles in the digestion of food or cuticle.

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Section: Discussionmentioning

confidence: 53%

“…A dual optimum pH toward glycolchitin has been reported for some fish stomach chitinases. 18,19,27) As shown in Fig. 3, HoChiA had the highest activity around pH 2 and exhibited a second optimum at pH 8 with 35% of the maximal activity at pH 2.…”

Section: N-terminal Amino Acid Sequences Of Greenling and Common Mackmentioning

confidence: 90%

Substrate Specificity of Chitinases from Two Species of Fish, Greenling,Hexagrammos otakii, and Common Mackerel,Scomber japonicus, and the Insect, Tobacco Hornworm,Manduca sexta

Matsumiya

Arakane

Haga

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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show abstract

“…12,15,38,39) Accordingly, the high temperature optimum and the thermal stability of the chitinase from Scorpaena scrofa provide further confirmation of its potential industrial application in the recycling of chitin wastes. 43) Substrate specificity of SsChi50 The ability to hydrolyze several carbohydrates substrates is an important criterion for the effectiveness of chitinases.…”

Section: )mentioning

confidence: 89%

“…These observations strongly suggest that SsChi50 from the red scorpionfish Scorpaena scrofa, like chitinases HoChi A, B, and C, is a monomeric protein comparable to other chitinases. 12,15,38,39) …”

Section: Molecular Weights Determination and Zymography Analysis Of Smentioning

confidence: 99%

Purification and Characterization of a Highly Thermostable Chitinase from the Stomach of the Red ScorpionfishScorpaena scrofawith Bioinsecticidal Activity toward Cowpea WeevilCallosobruchus maculatus(Coleoptera: Bruchidae)

Laribi-Habchi

Dziril

Badis

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…Red sea bream (Pagrus major) chitinase appeared to be involved in the digestion of chitin-containing foods [13]. In marine fishes of Monterey Bay, demersal species exhibited chitobiase activities and chitinase activities, which suggested that these fishes could degrade chitin completely to its soluble, absorbable monomer, Nacetyl-glucosamine [14].…”

Section: Introductionmentioning

confidence: 99%

Stimulatory effects of chitinase on growth and immune defense of orange-spotted grouper (Epinephelus coioides)

Zhang

Feng

Qin

et al. 2012

Fish & Shellfish Immunology

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Kinetic Analysis of a Chitinase from Red Sea Bream,Pagrus major

Cited by 17 publications

References 27 publications

Substrate Specificity of Chitinases from Two Species of Fish, Greenling,Hexagrammos otakii, and Common Mackerel,Scomber japonicus, and the Insect, Tobacco Hornworm,Manduca sexta

Substrate Specificity of Chitinases from Two Species of Fish, Greenling,Hexagrammos otakii, and Common Mackerel,Scomber japonicus, and the Insect, Tobacco Hornworm,Manduca sexta

Purification and Characterization of a Highly Thermostable Chitinase from the Stomach of the Red ScorpionfishScorpaena scrofawith Bioinsecticidal Activity toward Cowpea WeevilCallosobruchus maculatus(Coleoptera: Bruchidae)

Stimulatory effects of chitinase on growth and immune defense of orange-spotted grouper (Epinephelus coioides)

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