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大学・研究所にある論文を検索できる 「Enzymatic and structural studies of GH family 87 α-1,3-glucanase from Paenibacillus glycanilyticus FH11」の論文概要。リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。
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Enzymatic and structural studies of GH family 87 α-1,3-glucanase from Paenibacillus glycanilyticus FH11

INTUY Rattanaporn 立命館大学 DOI:info:doi/10.34382/00014045

2020.12.22

概要

α-1,3-Glucanase hydrolyzes α-1,3-glucan, an insoluble linear α-1,3-linked homopolymer of glucose that is found in the extracellular polysaccharides produced by oral Streptococcus mutans in dental plaque and fungal cell walls. This enzyme is expected to be of application in dental care and the development of fungal cell-wall lytic enzymes. In this study, two recombinant catalytic domains of α-1,3-glucanase isozymes, CatAglFH1 and CatAgl-FH2 from Paenibacillus glycanilyticus FH11, which is classified into glycoside hydrolase family 87, were prepared using a Brevibacillus choshinensis expression system and purified for enzymatic characterization and 3D structural analysis. CatAgl-FH1 and CatAgl-FH2, which consist of 574 and 580 amino acid residues, respectively, were purified. They showed specific activities of 0.70 U/mg and 0.77 U/mg, respectively. The molecular masses of both enzymes were estimated to be approximately 62 kDa by SDS-PAGE. Both recombinant enzymes exhibited the different properties in pH and temperature profiles. The optimal pH of CatAgl-FH1 and CatAgl-FH2 were 5.5 and 6.0, respectively. The optimal temperature of CatAgl-FH1 and CatAgl-FH2 were 60°C and 55°C, respectively. TLC analysis indicated that both recombinant enzymes exhibited substrate specificity towards α-1,3-glucan and showed endo-cleavage pattern. Major products of CatAgl-FH1 were di- and trisaccharide. In turns, the hydrolysis product of CatAgl-FH2 was mainly trisaccharide.

Both Agl-FH1 and Agl-FH2, the original enzymes, have multi-domain structure consisting of N-terminal substrate-binding domain and a C-terminal catalytic domain. The N-terminal of Agl-FH1 and Agl-FH2 showed each approximately 70% identity to the N-terminal moiety of Agl-KA from Bacillus circulans KA-304, and C-terminal of Agl-KA (CatAgl-KA) also exhibited highly similarity with CatAgl-FH2 sequence. Interestingly, the amino acid sequence of CatAgl-FH1 showed approximately 20% identity to CatAgl-KA and to those of the other known GH87 α-1,3-glucanases. No threedimensional structures of α-1,3-diglucanase has been available to date. Although crystal of full-length Agl-FH1 has not been obtained yet, crystals of Cat-Agl-FH1 were successfully prepared. The crystal structure of CatAgl-FH1 was analyzed by nativesingle-wavelength anomalous diffraction. The catalytic domain was composed of two modules, β-sandwich fold, and right-handed β-helix fold modules. The structure of βsandwich was similar to those of carbohydrate binding module (CBM) family 35 members. The crystal structure of CatAgl-FH1 were determined in complexed forms with or without oligosaccharides at 1.4 to 2.5 and 1.6 Å resolutions, respectively. The glycerolor α-1,3-diglucan (nigerose)-enzyme complex structures demonstrated that this βsandwich fold module was a novel carbohydrate binding module with the capabilities to bind saccharides and to promote the degradation of polysaccharides. The structure of inactive mutants in complexes with oligosaccharides showed that at least eight subsites for glucose binding are located in the active cleft of β-helix fold and the architecture of the active cleft was suitable for the recognition and hydrolysis of α-1,3-glucan with the inverting mechanism. The structural similarity with GH28 and GH49 enzymes and the site-directed mutagenesis indicate that three Asp residues, Asp1045, Asp1068, and Asp1069, are the most likely candidates for catalytic residues of Agl-FH1. It was also revealed that this enzyme hydrolyzed α-1,3-tetraglucan into glucose and α-1,3-triglucan with β-configuration at the reducing end by an inverting mechanism.

Both enzymes were tested to evaluate the capability of degrading or preventing for biofilm formed by S. mutans. Each enzyme was capable of preventing biofilm formation more than 70% in the culture medium at 16-h reaction time. The examination using laser scanning microscopy confirmed little biofilm adhere to surface of glass plate. In addition, both CatAgl-FH1 and CatAgl-FH2 degraded biofilm pre-formed on glass plate at 16 h with degradation efficiency of approximately 60% and 40%, respectively. The results showed that both enzymes have capability for dental care applications.

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