Synthesis of 4-methylcoumarin-7-yloxy tetra-N-acetyl-.BETA.-chitotetraoside, a novel synthetic substrate for the fluorometric assay of lysozyme.

Inaba, T.; Ohgushi, Tadayasu; Iga, Yoshiro; Hasegawa, Eiichi

doi:10.1248/cpb.32.1597

Cited by 23 publications

(9 citation statements)

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“…Chemical methods for the preparation of chitin oligomers include acid hydrolysis (25)(26)(27)(28)(29)(30)(31). Recently, series of chitin oligomers, up to the hexamer, have become commercially available.…”

Section: Preparation Of Chitin Oligomers By Chemical Hydrolysismentioning

confidence: 99%

Preparation of Chitin and Chitosan Oligomers and Their Applications in Physiological Functional Foods

Jeon¹,

Shahidi²,

Kim³

2000

Food Reviews International

228

116

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Section: Preparation Of Chitin Oligomers By Chemical Hydrolysismentioning

confidence: 99%

Preparation of Chitin and Chitosan Oligomers and Their Applications in Physiological Functional Foods

Jeon¹,

Shahidi²,

Kim³

2000

Food Reviews International

228

116

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“…p-Nitrophenyl (pNP)-␤-lacto-Nbioside I (LNB-␤-pNP) was obtained from Sigma-Aldrich or synthesized essentially as described previously (32). Briefly, hepta-Oacetyl-LNB was prepared by treating LNB with acetic anhydride and pyridine.…”

mentioning

confidence: 99%

Lacto-N-biosidase Encoded by a Novel Gene of Bifidobacterium longum Subspecies longum Shows Unique Substrate Specificity and Requires a Designated Chaperone for Its Active Expression

Sakurama

Kiyohara

Wada

et al. 2013

Journal of Biological Chemistry

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Background:Phenotypically lacto-N-biosidase-positive Bifidobacterium longum JCM1217 does not possess a gene homologous to previously identified lacto-N-biosidase. Results: Hypothetical proteins BLLJ_1505 and BLLJ_1506 encode lacto-N-biosidase and its designated chaperone, respectively. Conclusion:The enzyme showed unique and unexpected substrate specificity. Significance: The enzyme is important for understanding how B. longum consumes human milk oligosaccharides and also may serve as a new tool in glycobiology.

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“…Despite their biological interest and potential agronomical usefulness, CHOS with well-defined structures remain poorly accessible. CHOS with 2 to 6 degrees of polymerization (DP) were obtained from chitin by chemical or enzymatic depolymerization or metabolic engineering (2,17,30). Most biological activities require CHOS DP of Ն4 (12), but the synthesis of oligomers with Ն6 DP has been a daunting task.…”

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confidence: 99%

Synthesis of Long-Chain Chitooligosaccharides by a Hypertransglycosylating Processive Endochitinase of Serratia proteamaculans 568

Purushotham

Podile

2012

J Bacteriol

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We describe the heterologous expression and characterization of a 407-residue single-domain glycosyl hydrolase family 18 chitinase (SpChiD) from Gram-negative Serratia proteamaculans 568 that has unprecedented catalytic properties. SpChiD was optimally active at pH 6.0 and 40°C, where it showed a K m of 83 mg ml ؊1 , a k cat of 3.9 ؋ 10 2 h ؊1 , and a k cat /K m of 4.7 h mg ؊1 ml ؊1 on colloidal chitin. On chitobiose, the K m , k cat , and k cat /K m were 203 M, 1.3 ؋ 10 2 h ؊1 , and 0.62 h ؊1 M ؊1 , respectively. Hydrolytic activity on chitooligosaccharides (CHOS) and colloidal chitin indicated that SpChiD was an endo-acting processive enzyme, with the unique ability to convert released chitobiose to N-acetylglucosamine, the major end product. SpChiD showed hyper transglycosylation (TG) with trimer-hexamer CHOS substrates, generating considerable amounts of long-chain CHOS. The TG activity of SpChiD was dependent on both the length and concentration of the oligomeric substrate and also on the enzyme concentration. The length and amount of accumulated TG products increased with increases in the length of the substrate and its concentration and decreased with increases in the enzyme concentration. The SpChiD bound to insoluble and soluble chitin substrates despite the absence of accessory domains. Sequence alignments and structural modeling indicated that SpChiD would have a deep substrate-binding groove lined with aromatic residues, which is characteristic of processive enzymes. SpChiD shows a combination of properties that seems rare among family 18 chitinases and that may resemble the properties of human chitotriosidase.

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Synthesis of 4-methylcoumarin-7-yloxy tetra-N-acetyl-.BETA.-chitotetraoside, a novel synthetic substrate for the fluorometric assay of lysozyme.

Cited by 23 publications

References 0 publications

Preparation of Chitin and Chitosan Oligomers and Their Applications in Physiological Functional Foods

Preparation of Chitin and Chitosan Oligomers and Their Applications in Physiological Functional Foods

Lacto-N-biosidase Encoded by a Novel Gene of Bifidobacterium longum Subspecies longum Shows Unique Substrate Specificity and Requires a Designated Chaperone for Its Active Expression

Synthesis of Long-Chain Chitooligosaccharides by a Hypertransglycosylating Processive Endochitinase of Serratia proteamaculans 568

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