β-1,3-葡聚糖酶的结构、功能及应用研究进展

摘要/Abstract

摘要： β-1,3-葡聚糖酶是一类能够特异性水解β-1,3-葡聚糖中β-1,3-糖苷键的酶类，生成的产物为一系列不同大小的寡糖或单糖。β-1,3-葡聚糖酶在食品功能寡糖制备、果蔬保鲜、生物医药、植物抗病等领域具有重要应用价值。已发现的β-1,3-葡聚糖酶主要归属于12 个糖苷水解酶家族（glycoside hydrolases, GH），包括GH16、GH17、GH55、GH64、GH81、GH128和GH132等。β-1,3-葡聚糖酶广泛存在于细菌、真菌、植物和昆虫中，因来源和序列进化关系的差异，其结构和催化功能也呈现多样性。酶的结构与功能是探索酶催化反应机理、挖掘酶催化特性以及酶分子改造研究的基础。因此，本文从β-1,3-葡聚糖酶的结构、功能及应用等方面，对国内外β-1,3-葡聚糖酶的研究现状进行综述，以期为β-1,3-葡聚糖酶相关基础研究及应用开发提供参考。

关键词: β-1,3-葡聚糖酶, 糖苷水解酶, 结构与功能, 催化机制, 应用

Abstract: β-1,3-Glucanase, which has important potential applications in functional oligosaccharide preparation, fruit and vegetable preservation, biopharmaceuticals and plant disease resistance, specifically hydrolyzes β-1,3-glycosidic linkages in β-1,3-glucan, generating a range of oligosaccharides or monosaccharides. The known β-1, 3-glucanases belong to 12 glycoside hydrolases (glycoside hydrolases, GH) families, including GH16, GH17, GH55, GH64, GH81, GH128 and GH132, et al. β-1,3-Glucanases are widely distributed in bacteria, fungi, plants and insects, which exhibit diversified structures and catalytic functions due to differences in sources and sequence evolution. Structural and functional studies of enzymes are the basis for exploring the catalytic mechanism, enzyme properties, and molecular modification. ?Therefore, this paper reviews the domestic and abroad current research progress on structure, function and application of β-1, 3-glucanases, in order to provide references for theoretical research and application development related to β-1,3-glucanases.

Key words: β-1,3-glucanase, glycoside hydrolase, structure and function, catalytic mechanism, application

魏夏森余赛男张哲一高海燕秦臻. β-1,3-葡聚糖酶的结构、功能及应用研究进展[J]. 食品科学, 0, (): 0-0.

参考文献

[1] KADAM S U, TIWARI B K, O'DONNELL C P. Extraction, structure and biofunctional activities of laminarin from brown algae [J]. International Journal of Food Science and Technology, 2015, 50(1): 24-31. [2] MIYOSHI K, UEZU K, SAKURAI K, et al. Proposal of a new hydrogen-bonding form to maintain curdlan triple helix [J]. Chemistry & Biodiversity, 2004, 1(6): 916-24. [3] 傅赟彬, 赵小明, 杜昱光. 可德兰多糖及其衍生物的生物活性和应用研究进展 [J]. 食品科学, 2012, 33(07): 315-9. [4] SHIMIZU J, TSUCHIHASHI N, KUDOH K, et al. Dietary curdlan increases proliferation of bifidobacteria in the cecum of rats [J]. Bioscience Biotechnology and Biochemistry, 2001, 65(2): 466-9. [5] 于永华, 徐飞飞, 林琳, et al. 燕麦β-葡聚糖降血脂作用的研究进展 [J]. 临床与病理杂志, 2022, 42(02): 486-91. [6] DAVIES G, HENRISSAT B. Structures and mechanisms of glycosyl hydrolases [J]. Structure (London, England : 1993), 1995, 3(9): 853-9. [7] ILARI A, FIORILLO A, ANGELACCIO S, et al. Crystal structure of a famil16 endoglucanase from the hyperthermophile basis of substrate recognition [J]. FEBS Journal, 2009, 276(4): 1048-58. [8] YUAN Y, ZHANG X, ZHANG H, et al. Degradative GH5 β-1,3-1,4-glucanase PpBglu5A for glucan in Paenibacillus polymyxa KF-1 [J]. Process Biochemistry, 2020, 98: 183-92. [9] JAAFAR N R, KHOIRI N M, ISMAIL N F, et al. Functional characterisation and product specificity of Endo-β-1,3-glucanase from alkalophilic bacterium, Bacillus lehensis G1 [J]. Enzyme and Microbial Technology, 2020, 140. [10] SHI P, YAO G, YANG P, et al. Cloning, characterization, and antifungal activity of an endo-1,3-β-d-glucanase from Streptomyces sp. S27 [J]. Applied Microbiology and Biotechnology, 2009, 85(5): 1483-90. [11] HARTL L, GASTEBOIS A, AIMANIANDA V, et al. Characterization of the GPI-anchored endo β-1,3-glucanase Eng2 of Aspergillus fumigatus [J]. Fungal Genetics and Biology, 2011, 48(2): 185-91. [12] DA SILVA AIRES R, STEINDORFF A S, RAMADA M H S, et al. Biochemical characterization of a 27kDa 1,3-β-d-glucanase from Trichoderma asperellum induced by cell wall of Rhizoctonia solani [J]. Carbohydrate Polymers, 2012, 87(2): 1219-23. [13] ISHIDA T, FUSHINOBU S, KAWAI R, et al. Crystal Structure of Glycoside Hydrolase Family 55 β-1,3-Glucanase from the Basidiomycete Phanerochaete chrysosporium [J]. Journal of Biological Chemistry, 2009, 284(15): 10100-9. [14] VARGHESE J N, GARRETT T P, COLMAN P M, et al. Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities [J]. Proceedings of the National Academy of Sciences of the United States of America, 1994, 91(7): 2785-9. [15] ROMERO I, FERNANDEZ-CABALLERO C, GONI O, et al. Functionality of a class I beta-1,3-glucanase from skin of table grapes berries [J]. Plant Science, 2008, 174(6): 641-8. [16] YU W Q, ZHENG G P, QIU D W, et al. Paenibacillus terrae NK3-4: A potential biocontrol agent that produces β-1,3-glucanase [J]. Biological Control, 2019, 129: 92-101. [17] LI C, WEN Y, HE Y, et al. Purification and characterization of a novel β-1,3-glucanase from Arca inflata and its immune-enhancing effects [J]. Food Chemistry, 2019, 290: 1-9. [18] GAO M-J, YAN J-J, ZHAO Y, et al. Expression of a thermostable β-1,3-glucanase from Trichoderma harzianum in Pichia pastoris and use in oligoglucosides hydrolysis [J]. Process Biochemistry, 2021, 107: 74-82. [19] ZHANG D, SPADARO D, VALENTE S, et al. Cloning, characterization and expression of an exo-1,3-β-glucanase gene from the antagonistic yeast, Pichia guilliermondii strain M8 against grey mold on apples [J]. Biological Control, 2011, 59(2): 284-93. [20] KALYANI D C, REICHENBACH T, ASPEBORG H, et al. A homodimeric bacterial exo-beta-1,3-glucanase derived from moose rumen microbiome shows a structural framework similar to yeast exo-beta-1,3-glucanases [J]. Enzyme Microb Technol, 2021, 143: 109723. [21] YI P, YAN Q, JIANG Z, et al. A first glycoside hydrolase family 50 endo-β-1,3-d-glucanase from Pseudomonas aeruginosa [J]. Enzyme and Microbial Technology, 2018, 108: 34-41. [22] WANG Y, ZHAO Y, WANG X, et al. Functional Characterization of the Novel Laminaripentaose-Producing β-1,3-Glucanase MoGluB and Its Biocontrol of Magnaporthe oryzae [J]. Journal of Agricultural and Food Chemistry, 2021, 69(33): 9571-84. [23] 程政翔. β-1,3-葡聚糖酶在毕赤酵母中的表达 [D]; 哈尔滨工业大学, 2013. [24] VUONG T V, WILSON D B. Glycoside Hydrolases: Catalytic Base/Nucleophile Diversity [J]. Biotechnology and Bioengineering, 2010, 107(2): 195-205. [25] WOJTKOWIAK A, WITEK K, HENNIG J, et al. Structures of an active-site mutant of a plant 1,3-β-glucanase in complex with oligosaccharide products of hydrolysis [J]. Acta Crystallographica Section D Biological Crystallography, 2012, 69(1): 52-62. [26] WU H-M, LIU S-W, HSU M-T, et al. Structure, Mechanistic Action, and Essential Residues of a GH-64 Enzyme, Laminaripentaose-producing β-1,3-Glucanase [J]. Journal of Biological Chemistry, 2009, 284(39): 26708-15. [27] QIN Z, YANG D, YOU X, et al. The recognition mechanism of triple-helical β-1,3-glucan by a β-1,3-glucanase [J]. Chemical Communications, 2017, 53(67): 9368-71. [28] GHOSH R, CHAKRABARTI C. Crystal structure analysis of NP24-I: a thaumatin-like protein [J]. Planta, 2008, 228(5): 883-90. [29] HENRISSAT B, GARRON M-L. How a Glycoside Hydrolase Recognizes a Helical Polyglucan [J]. Structure, 2017, 25(9): 1319-21. [30] PLUVINAGE B, FILLO A, MASSEL P, et al. Structural Analysis of a Family 81 Glycoside Hydrolase Implicates Its Recognition of beta-1,3-Glucan Quaternary Structure [J]. Structure, 2017, 25(9): 1348-+. [31] KUMAR K, CORREIA M A S, PIRES V M R, et al. Novel insights into the degradation of β-1,3-glucans by the cellulosome of Clostridium thermocellum revealed by structure and function studies of a family 81 glycoside hydrolase [J]. International Journal of Biological Macromolecules, 2018, 117: 890-901. [32] ZHOU P, CHEN Z Z, YAN Q J, et al. The structure of a glycoside hydrolase family 81 endo-beta-1,3-glucanase [J]. Acta Crystallographica Section D-Structural Biology, 2013, 69: 2027-38. [33] MA J, QIN Z, ZHOU P, et al. Structural insights into the substrate recognition and catalytic mechanism of a fungal glycoside hydrolase family 81 β-1,3-glucanase [J]. Enzyme and Microbial Technology, 2022, 153. [34] BIANCHETTI C M, TAKASUKA T E, DEUTSCH S, et al. Active Site and Laminarin Binding in Glycoside Hydrolase Family 55 [J]. Journal of Biological Chemistry, 2015, 290(19): 11819-32. [35] PAPAGEORGIOU A C, CHEN J, LI D. Crystal structure and biological implications of a glycoside hydrolase family 55 β-1,3-glucanase from Chaetomium thermophilum [J]. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2017, 1865(8): 1030-8. [36] SANTOS C R, COSTA P, VIEIRA P S, et al. Structural insights into beta-1,3-glucan cleavage by a glycoside hydrolase family [J]. Nature Chemical Biology, 2020, 16(8): 920-+. [37] GASTEBOIS A, AIMANIANDA V, BACHELLIER-BASSI S, et al. SUN Proteins Belong to a Novel Family of beta-(1,3)-Glucan-modifying Enzymes Involved in Fungal Morphogenesis [J]. Journal of Biological Chemistry, 2013, 288(19): 13387-96. [38] DéJEAN G, TAMURA K, CABRERA A, et al. Synergy between Cell Surface Glycosidases and Glycan-Binding Proteins Dictates the Utilization of Specific Beta(1,3)-Glucans by Human Gut Bacteroides [J]. mBio, 2020, 11(2). [39] 娄树宝, 彭东君, 王辉. 大豆β-1,3-葡聚糖酶的抑菌活性 [J]. 黑龙江八一农垦大学学报, 2008(03):27-29. [40] 陈小云, 李坚斌, 林莹, et al. β-1,3-葡聚糖酶和几丁质酶在热带水果保鲜中的应用[J].食品工业科技 [J]. 食品工业科技, 2008(05):294-296. [41] RAJNINEC M, FRATRIKOVA M, BOSZORADOVA E, et al. Basic β-1,3-Glucanase from Drosera binata Exhibits Antifungal Potential in Transgenic Tobacco Plants [J]. Plants, 2021, 10(8). [42] LI K, CHEN W, WANG W, et al. Effective degradation of curdlan powder by a novel endo-β-1→3-glucanase [J]. Carbohydrate Polymers, 2018, 201: 122-30. [43] 吕丽丽, 王瑞宾, 王家林, 等. 高效β-葡聚糖酶对麦汁过滤速度的影响 [J]. 酿酒科技, 2010(3):3. [44] 林开江, 阮丽娟, 王龙英. 用纤维素酶制备酵母菌原生质体的研究 [J]. 科技通报, 1996, 12(2):4. [45] 段会轲, 熊善柏, 刘海梅. 酵母β-1,3-葡聚糖的酶法增溶及产物分析 [J]. 食品科学, 2008, 29(1):5. [46] NETT J, LINCOLN L, MARCHILLO K, et al. Putative Role of β-1,3 Glucans in Candida albicans Biofilm Resistance [J]. Antimicrobial Agents and Chemotherapy, 2007, 51(2): 510-20. [47] MITCHELL K F, TAFF H T, CUEVAS M A, et al. Role of Matrix β-1,3 Glucan in Antifungal Resistance of Non-albicans Candida Biofilms [J]. Antimicrobial Agents and Chemotherapy, 2013, 57(4): 1918-20.