Abstract
Lignocellulosic biomass, which mainly consists of cellulose and hemicellulose, is the most abundant renewable biopolymer on earth. β-Glucanases are glycoside hydrolases (GHs) that hydrolyze β-glucan, one of the dominant components of the plant cell wall, into cello-oligosaccharides and glucose. Among them, endo-β-1,4-glucanase (EC 3.2.1.4), exo-glucanase/cellobiohydrolase (EC 3.2.1.91), and β-glucosidase (EC 3.2.1.21) play critical roles in the digestion of glucan-like substrates. β-Glucanases have attracted considerable interest within the scientific community due to their applications in the feed, food, and textile industries. In the past decade, there has been considerable progress in the discovery, production, and characterization of novel β-glucanases. Advances in the development of next-generation sequencing techniques, including metagenomics and metatranscriptomics, have unveiled novel β-glucanases isolated from the gastrointestinal microbiota. The study of β-glucanases is beneficial for research and development of commercial products. In this study, we review the classification, properties, and engineering of β-glucanases.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Abdeev RM, Abdeeva IA, Bruskin SS, Musiychuk KA, Goldenkova-Pavlova IV, Piruzian ES (2009) Bacterial thermostable β-glucanases as a tool for plant functional genomics. Gene 436:81–89. https://doi.org/10.1016/j.gene.2009.01.021
Adsul M, Sandhu SK, Singhania RR, Gupta R, Puri SK, Mathur A (2020) Designing a cellulolytic enzyme cocktail for the efficient and economical conversion of lignocellulosic biomass to biofuels. Enzyme Microb Technol 133:109442. https://doi.org/10.1016/j.enzmictec.2019.109442
Alnadari F, Xue Y, Almakas A, Mohedein A, Samie A, Abdel-Shafi M, Abdin M (2020a) Large batch production of galactooligosaccharides using β-glucosidase immobilized on chitosan-functionalized magnetic nanoparticle. J Food Biochem 45:e13589. https://doi.org/10.1111/jfbc.13589
Alnadari F, Xue Y, Zhou L, Hamed YS, Taha M, Foda MF (2020b) Immobilization of β-glucosidase from Thermatoga maritima on chitin-functionalized magnetic nanoparticle via a novel thermostable chitin-binding domain. Sci Rep 10:1663. https://doi.org/10.1038/s41598-019-57165-5
Anderson KL, Salyers AA (1989) Biochemical evidence that starch breakdown by Bacteroides thetaiotaomicron involves outer membrane starch-binding sites and periplasmic starch-degrading enzymes. J Bacteriol 171:3192–3198. https://doi.org/10.1128/jb.171.6.3192-3198.1989
Ariaeenejad S, Mamaghani ASA, Maleki M, Kavousi K, Shahraki MF, Salekdeh GH (2020) A novel high performance in-silico screened metagenome-derived alkali-thermostable endo-β-1,4-glucanase for lignocellulosic biomass hydrolysis in the harsh conditions. BMC Biotechnol 20:56. https://doi.org/10.1186/s12896-020-00647-6
Arnold FH, Wintrode PL, Miyazaki K, Gershenson A (2001) How enzymes adapt: lessons from directed evolution. Trends Biochem Sci 26:100–106. https://doi.org/10.1016/s0968-0004(00)01755-2
Baba Y, Matsuki Y, Takizawa S, Suyama Y, Tada C, Fukuda Y, Saito M, Nakai Y (2019) Pretreatment of lignocellulosic biomass with cattle rumen fluid for methane production: fate of added rumen microbes and indigenous microbes of methane seed sludge. Microbes Environ 34:421–428. https://doi.org/10.1264/jsme2.ME19113
Bai L, Kim J, Son KH, Shin DH, Ku BH, Kim DY, Park HY (2021) Novel anti-fungal d-laminaripentaose-releasing endo-β-1,3-glucanase with a RICIN-like domain from Cellulosimicrobium funkei HY-13. Biomolecules 11:1080. https://doi.org/10.3390/biom11081080
Banner A, Toogood HS, Scrutton NS (2021) Consolidated bioprocessing: synthetic biology routes to fuels and fine chemicals. Microorganisms 9(5):1079. https://doi.org/10.3390/microorganisms9051079
Brown HA, Koropatkin NM (2021) Host glycan utilization within the Bacteroidetes Sus-like paradigm. Glycobiology 31:697–706. https://doi.org/10.1093/glycob/cwaa054
Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:D233–D238. https://doi.org/10.1093/nar/gkn663
Cao JW, Deng Q, Gao DY, He B, Yin SJ, Qian LC, Wang JK, Wang Q (2021) A novel bifunctional glucanase exhibiting high production of glucose and cellobiose from rumen bacterium. Int J Biol Macromol 173:136–145. https://doi.org/10.1016/j.ijbiomac.2021.01.113
Cecchini DA, Pepe O, Pennacchio A, Fagnano M, Faraco V (2018) Directed evolution of the bacterial endo-β-1,4-glucanase from Streptomyces sp. G12 towards improved catalysts for lignocellulose conversion. AMB Express 8:74. https://doi.org/10.1186/s13568-018-0602-7
Cerda LA, Valenzuela SV, Diaz P, Pastor FI (2016) New GH16 β-glucanase from Paenibacillus barcinonensis BP-23 releases a complex pattern of mixed-linkage oligomers from barley glucan. Biotechnol Appl Biochem 63:51–56. https://doi.org/10.1002/bab.1348
Chai S, Zhang X, Gao Y, Nie L, Xiang C, Cao M, Wang S, Feng Z (2021) Identification and characterization of a novel endo-β-1,4-glucanase from a soil metagenomic library. Carbohydr Res 510:108460. https://doi.org/10.1016/j.carres.2021.108460
Choi H, Han J, Lee J (2021) Renewable butanol production via catalytic routes. Int J Environ Res Public Health 18(22):11749. https://doi.org/10.3390/ijerph182211749
Cuskin F, Lowe EC, Temple MJ, Zhu Y, Cameron E, Pudlo NA, Porter NT, Urs K, Thompson AJ, Cartmell A, Rogowski A, Hamilton BS, Chen R, Tolbert TJ, Piens K, Bracke D, Vervecken W, Hakki Z, Speciale G, Munoz-Munoz JL, Day A, Pena MJ, McLean R, Suits MD, Boraston AB, Atherly T, Ziemer CJ, Williams SJ, Davies GJ, Abbott DW, Martens EC, Gilbert HJ (2015) Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism. Nature 517:165–169. https://doi.org/10.1038/nature13995
Dadheech T, Shah R, Pandit R, Hinsu A, Chauhan PS, Jakhesara S, Kunjadiya A, Rank D, Joshi C (2018) Cloning, molecular modeling and characterization of acidic cellulase from buffalo rumen and its applicability in saccharification of lignocellulosic biomass. Int J Biol Macromol 113:73–81. https://doi.org/10.1016/j.ijbiomac.2018.02.100
Deflandre B, Jadot C, Planckaert S, Thiébaut N, Stulanovic N, Herman R, Devreese B, Kerff F, Rigali S (2022) Structure and function of BcpE2, the most promiscuous GH3-family glucose scavenging β-glucosidase. mBio 13:e0093522. https://doi.org/10.1128/mbio.00935-22
Dejean G, Tamura K, Cabrera A, Jain N, Pudlo NA, Pereira G, Viborg AH, Van Petegem F, Martens EC, Brumer H (2020) Synergy between cell surface glycosidases and glycan-binding proteins dictates the utilization of specific β(1,3)-glucans by human gut Bacteroides. mBio 11(2):e00095-20. https://doi.org/10.1128/mBio.00095-20
Ding Y, Zhang H, Wang X, Zu H, Wang C, Dong D, Lyu M, Wang S (2020) Immobilization of dextranase on nano-hydroxyapatite as a recyclable catalyst. Materials 14:130. https://doi.org/10.3390/ma14010130
Gao DY, Sun XB, Liu MQ, Liu YN, Zhang HE, Shi XL, Li YN, Wang JK, Yin SJ, Wang Q (2019) Characterization of thermostable and chimeric enzymes via isopeptide bond-mediated molecular cyclization. J Agric Food Chem 67:6837–6846. https://doi.org/10.1021/acs.jafc.9b01459
Gao DY, Sun XB, Fang Y, He B, Wang JH, Liu JX, Wang JK, Wang Q (2022) Heterologous expression and characterization of two novel glucanases derived from sheep rumen microbiota. World J Microbiol Biotechnol 38:87. https://doi.org/10.1007/s11274-022-03269-6
Garfoot AL, Dearing KL, VanSchoiack AD, Wysocki VH, Rappleye CA (2017) Eng1 and Exg8 are the major β-glucanases secreted by the fungal pathogen Histoplasma capsulatum. J Biol Chem 292:4801–4810. https://doi.org/10.1074/jbc.M116.762104
Gavande PV, Kumar K, Ahmed J, Goyal A (2023) Multifunctionality and mechanism of processivity of family GH5 endoglucanase, RfGH5_4 from Ruminococcus flavefaciens on lignocellulosic polymers. Int J Biol Macromol 224:1395–1411. https://doi.org/10.1016/j.ijbiomac.2022.10.227
Ghali I, Sofyan A, Ohmori H, Shinkai T, Mitsumori M (2017) Diauxic growth of Fibrobacter succinogenes S85 on cellobiose and lactose. FEMS Microbiol Lett 364(15):fnx150. https://doi.org/10.1093/femsle/fnx150
Ghio S, Bradanini MB, Garrido MM, Ontanon OM, Piccinni FE, Marrero Diaz de Villegas R, Talia PM, Campos E (2020) Synergic activity of Cel8Pa β-1,4 endoglucanase and Bg1Pa β-glucosidase from Paenibacillus xylanivorans A59 in β-glucan conversion. Biotechnol Rep 28:e00526. https://doi.org/10.1016/j.btre.2020.e00526
Gu Y, Zheng F, Wang Y, Su X, Bai Y, Yao B, Huang H, Luo H (2019) Characterization of two thermophilic cellulases from Talaromyces leycettanus JCM12802 and their synergistic action on cellulose hydrolysis. PLoS ONE 14:e0224803. https://doi.org/10.1371/journal.pone.0224803
Guerrero EB, de Villegas RMD, Soria MA, Santangelo MP, Campos E, Talia PM (2020) Characterization of two GH5 endoglucanases from termite microbiome using synthetic metagenomics. Appl Microbiol Biotechnol 104:8351–8366. https://doi.org/10.1007/s00253-020-10831-5
Han J, Feng H, Wu J, Li Y, Zhou Y, Wang L, Luo P, Wang Y (2021) Construction of multienzyme co-immobilized hybrid nanoflowers for an efficient conversion of cellulose into glucose in a cascade reaction. J Agric Food Chem 69:7910–7921. https://doi.org/10.1021/acs.jafc.1c02056
Hantani Y, Motoki S, Miyagawa A, Yamamura H, Oda M (2018) Transglycosylation activity of catalytic domain mutant of endo-1,3-β-glucanase from Cellulosimicrobium cellulans. Protein Pept Lett 25:734–739. https://doi.org/10.2174/0929866525666180704094109
Hou L, Ji D, Dong W, Yuan L, Zhang F, Li Y, Zang L (2020) The synergistic action of electro-fenton and white-rot fungi in the degradation of lignin. Front Bioeng Biotechnol 8:99. https://doi.org/10.3389/fbioe.2020.00099
Huang Z, Ni G, Zhao X, Wang F, Qu M (2021) Characterization of a GH8 β-1,4-glucanase from Bacillus subtilis B111 and its saccharification potential for agricultural straws. J Microbiol Biotechnol 31:1446–1454. https://doi.org/10.4014/jmb.2105.05026
Jaafar NR, Khoiri NM, Ismail NF, Mahmood NAN, Abdul Murad AM, Abu Bakar FD, Mat Yajit NL, Illias RM (2020) Functional characterisation and product specificity of endo-β-1,3-glucanase from alkalophilic bacterium, Bacillus lehensis G1. Enzyme Microb Technol 140:109625. https://doi.org/10.1016/j.enzmictec.2020.109625
Jiang N, Ma XD, Fu LH, Li CX, Feng JX, Duan CJ (2020) Identification of a unique 1,4-β-D-glucan glucohydrolase of glycoside hydrolase family 9 from Cytophaga hutchinsonii. Appl Microbiol Biotechnol 104:7051–7066. https://doi.org/10.1007/s00253-020-10731-8
Kalyani DC, Reichenbach T, Aspeborg H, Divne C (2021) A homodimeric bacterial exo-β-1,3-glucanase derived from moose rumen microbiome shows a structural framework similar to yeast exo-β-1,3-glucanases. Enzyme Microb Technol 143:109723. https://doi.org/10.1016/j.enzmictec.2020.109723
Kang HJ, Coulibaly F, Clow F, Proft T, Baker EN (2007) Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Science 318:1625–1628. https://doi.org/10.1126/science.1145806
Kim SK, Chung D, Himmel ME, Bomble YJ, Westpheling J (2019) Heterologous co-expression of two β-glucanases and a cellobiose phosphorylase resulted in a significant increase in the cellulolytic activity of the Caldicellulosiruptor bescii exoproteome. J Ind Microbiol Biotechnol 46:687–695. https://doi.org/10.1007/s10295-019-02150-0
Kim DY, Kim J, Lee YM, Byeon SM, Gwak JH, Lee JS, Shin DH, Park HY (2022) Novel, acidic, and cold-adapted glycoside hydrolase family 8 endo-β-1,4-glucanase from an Antarctic lichen-associated bacterium, Lichenicola cladoniae PAMC 26568. Front Microbiol 13:935497. https://doi.org/10.3389/fmicb.2022.935497
Kuchner O, Arnold FH (1997) Directed evolution of enzyme catalysts. Trends Biotechnol 15:523–530. https://doi.org/10.1016/s0167-7799(97)01138-4
Lamed K, Bayer EA (1983) Cellulosome: a discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities. Biotechnol Bioeng Symp 13:163–181
Leung DW, Chen E, Goeddel DV (1989) A method for Random Mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1:11–15
Li YX, Yi P, Yan QJ, Qin Z, Liu XQ, Jiang ZQ (2017) Directed evolution of a β-mannanase from Rhizomucor miehei to improve catalytic activity in acidic and thermophilic conditions. Biotechnol Biofuels 10:143. https://doi.org/10.1186/s13068-017-0833-x
Li J, Cao C, Jiang Y, Huang Q, Shen Y, Ni J (2020) A novel digestive GH16 β-1,3(4)-glucanase from the fungus-growing termite Macrotermes barneyi. Appl Biochem Biotechnol 192:1284–1297. https://doi.org/10.1007/s12010-020-03368-w
Li H, Hu Q, Hong X, Jiang Z, Ni H, Li Q, Zhu Y (2021a) Molecular cloning and characterization of a thermostable and halotolerant endo-β-1,4-glucanase from Microbulbifer sp. ALW1. 3 Biotech 11:250. https://doi.org/10.1007/s13205-021-02801-z
Li Z, Niu C, Yang X, Zheng F, Liu C, Wang J, Li Q (2021b) Enhanced acidic resistance ability and catalytic properties of Bacillus 1,3-1,4-β-glucanases by sequence alignment and surface charge engineering. Int J Biol Macromol 192:426–434. https://doi.org/10.1016/j.ijbiomac.2021.10.008
Li Y, Song W, Han X, Wang Y, Rao S, Zhang Q, Zhou J, Li J, Liu S, Du G (2022) Recent progress in key lignocellulosic enzymes: enzyme discovery, molecular modifications, production, and enzymatic biomass saccharification. Bioresour Technol 363:127986. https://doi.org/10.1016/j.biortech.2022.127986
Lin Y, Jin W, Cai L, Liu X, Qiu Y, Zhang G (2021) Green preparation of covalently co-immobilized multienzymes on silica nanoparticles for clean production of reducing sugar from lignocellulosic biomass. J Clean Prod 314. https://doi.org/10.1016/j.jclepro.2021.127994
Liu ZL, Dien BS (2022) Cellulosic ethanol production using a dual functional novel yeast. Int J Microbiol 2022:7853935. https://doi.org/10.1155/2022/7853935
Liu X, Wang R, Bi J, Kang L, Zhou J, Duan B, Liu Z, Yuan S (2020) A novel endo-β-1,6-glucanase from the mushroom Coprinopsis cinerea and its application in studying of cross-linking of β-1,6-glucan and the wall extensibility in stipe cell walls. Int J Biol Macromol 160:612–622. https://doi.org/10.1016/j.ijbiomac.2020.05.244
Liu C, Yan S, Zhao J, Lin M, Duan B, Zhang Z, Yang Y, Liu Z, Yuan S (2021) An aspergillus nidulans endo-β-1,3-glucanase exhibited specific catalytic features and was used to prepare 3-O-β-cellobiosyl-d-glucose and 3-O-β-gentiobiosyl-d-glucose with high antioxidant activity from barley β-glucan and laminarin, respectively. Int J Biol Macromol 186:424–432. https://doi.org/10.1016/j.ijbiomac.2021.07.053
Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS (2002) Microbial cellulose utilization: Fundamentals and biotechnology. Microbiol Mol Biol Rev 66:506–577. https://doi.org/10.1128/MMBR.66.3.506-577.2002
Ma J, Li Y, Han S, Jiang Z, Yan Q, Yang S (2021) Structural and biochemical insights into the substrate-binding mechanism of a glycoside hydrolase family 12 β-1,3-1,4-glucanase from Chaetomium sp. J Struct Biol 213:107774. https://doi.org/10.1016/j.jsb.2021.107774
Mafa MS, Dirr HW, Malgas S, Krause RWM, Rashamuse K, Pletschke BI (2020a) A novel dimeric exoglucanase (GH5_38): biochemical and structural characterisation towards its application in alkyl cellobioside synthesis. Molecules 25(3):746. https://doi.org/10.3390/molecules25030746
Mafa MS, Malgas S, Rashamuse K, Pletschke BI (2020b) Delineating functional properties of a cello-oligosaccharide and β-glucan specific cellobiohydrolase (GH5_38): its synergism with Cel6A and Cel7A for β-(1,3)-(1,4)-glucan degradation. Carbohydr Res 495:108081. https://doi.org/10.1016/j.carres.2020.108081
Matsuzawa T, Kameyama A, Nakamichi Y, Yaoi K (2020) Identification and characterization of two xyloglucan-specific endo-1,4-glucanases in aspergillus oryzae. Appl Microbiol Biotechnol 104:8761–8773. https://doi.org/10.1007/s00253-020-10883-7
Nagy T, Tunnicliffe RB, Higgins LD, Walters C, Gilbert HJ, Williamson MP (2007) Characterization of a double dockerin from the cellulosome of the anaerobic fungus Piromyces equi. J Mol Biol 373:612–622. https://doi.org/10.1016/j.jmb.2007.08.007
Ohara H, Noguchi J, Karita S, Kimura T, Sakka K, Ohmiya K (2000) Sequence of egV and properties of EgV, a Ruminococcus albus endoglucanase containing a dockerin domain. Biosci Biotechnol Biochem 64:80–88. https://doi.org/10.1271/bbb.64.80
Ohta T, Horie H, Matsu-Ura A, Kawai F (2019) Cloning, expression, and characterization of novel GH5 endoglucanases from Thermobifida alba AHK119. J Biosci Bioeng 127:554–562. https://doi.org/10.1016/j.jbiosc.2018.10.015
Phakeenuya V, Ratanakhanokchai K, Kosugi A, Tachaapaikoon C (2020) A novel multifunctional GH9 enzyme from Paenibacillus curdlanolyticus B-6 exhibiting endo/exo functions of cellulase, mannanase and xylanase activities. Appl Microbiol Biotechnol 104:2079–2096. https://doi.org/10.1007/s00253-020-10388-3
Plakys G, Gasparaviciute R, Vaitekunas J, Rutkiene R, Meskys R (2022) Characterization of Paenibacillus sp. GKG endo-β-1, 3-glucanase, a member of family 81 glycoside hydrolases. Microorganisms 10:1930. https://doi.org/10.3390/microorganisms10101930
Rykov SV, Kornberger P, Herlet J, Tsurin NV, Zorov IN, Zverlov VV, Liebl W, Schwarz WH, Yarotsky SV, Berezina OV (2019) Novel endo-(1,4)-β-glucanase Bgh12A and xyloglucanase Xgh12B from aspergillus cervinus belong to GH12 subgroup I and II, respectively. Appl Microbiol Biotechnol 103:7553–7566. https://doi.org/10.1007/s00253-019-10006-x
Sadaqat B, Sha C, Rupani PF, Wang H, Zuo W, Shao W (2021) Man/Cel5B, a bifunctional enzyme having the highest mannanase activity in the hyperthermic environment. Front Bioeng Biotechnol 9:637649. https://doi.org/10.3389/fbioe.2021.637649
Sechovcova H, Kulhava L, Fliegerova K, Trundova M, Morais D, Mrazek J, Kopecny J (2019) Comparison of enzymatic activities and proteomic profiles of Butyrivibrio fibrisolvens grown on different carbon sources. Proteome Sci 17:2. https://doi.org/10.1186/s12953-019-0150-3
Shukla A, Gundampati RK, Jagannadham MV (2017) Immobilization of Euphorbia tirucalli peroxidase onto chitosan-cobalt oxide magnetic nanoparticles and optimization using response surface methodology. Int J Biol Macromol 102:384–395. https://doi.org/10.1016/j.ijbiomac.2017.03.153
Sohail M, Barzkar N, Michaud P, Tamadoni Jahromi S, Babich O, Sukhikh S, Das R, Nahavandi R (2022) Cellulolytic and xylanolytic enzymes from yeasts: properties and industrial applications. Molecules 27(12):1783. https://doi.org/10.3390/molecules27123783
Song WJ, Yu J, Tezcan FA (2017) Importance of scaffold flexibility/rigidity in the design and directed evolution of artificial metallo-β-lactamases. J Am Chem Soc 139:16772–16779. https://doi.org/10.1021/jacs.7b08981
Stemmer WP (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389–391. https://doi.org/10.1038/370389a0
Sulman AM, Matveeva VG, Bronstein LM (2022) Cellulase immobilization on nanostructured supports for biomass waste processing. Nanomaterials 12:3796. https://doi.org/10.3390/nano12213796
Sun XB, Cao JW, Wang JK, Lin HZ, Gao DY, Qian GY, Park YD, Chen ZF, Wang Q (2019a) SpyTag/SpyCatcher molecular cyclization confers protein stability and resilience to aggregation. Nat Biotechnol 49:28–36. https://doi.org/10.1016/j.nbt.2018.12.003
Sun Z, Liu Q, Qu G, Feng Y, Reetz MT (2019b) Utility of B-factors in protein science: interpreting rigidity, flexibility, and internal motion and engineering thermostability. Chem Rev 119:1626–1665. https://doi.org/10.1021/acs.chemrev.8b00290
Sun ZB, Xu JL, Lu X, Zhang W, Ji C, Ren Q (2020) Directed mutation of β-glucanases from probiotics to enhance enzymatic activity, thermal and pH stability. Arch Microbiol 202:1749–1756. https://doi.org/10.1007/s00203-020-01886-z
Sun XB, Gao DY, Cao JW, Liu Y, Rong ZT, Wang JK, Wang Q (2023) BsLPMO10A from Bacillus subtilis boosts the depolymerization of diverse polysaccharides linked via β-1,4-glycosidic bonds. Int J Biol Macromol 230:123133. https://doi.org/10.1016/j.ijbiomac.2023.123133
Tamura K, Foley MH, Gardill BR, Dejean G, Schnizlein M, Bahr CME, Louise Creagh A, van Petegem F, Koropatkin NM, Brumer H (2019) Surface glycan-binding proteins are essential for cereal β-glucan utilization by the human gut symbiont Bacteroides ovatus. Cell Mol Life Sci 76:4319–4340. https://doi.org/10.1007/s00018-019-03115-3
Temple MJ, Cuskin F, Basle A, Hickey N, Speciale G, Williams SJ, Gilbert HJ, Lowe EC (2017) A Bacteroidetes locus dedicated to fungal 1,6-β-glucan degradation: unique substrate conformation drives specificity of the key endo-1,6-β-glucanase. J Biol Chem 292:10639–10650. https://doi.org/10.1074/jbc.M117.787606
Torktaz I, Karkhane AA, Hemmat J (2018) Rational engineering of Cel5E from Clostridium thermocellum to improve its thermal stability and catalytic activity. Appl Microbiol Biotechnol 102:8389–8402. https://doi.org/10.1007/s00253-018-9204-1
Urbanowicz BR, Bennett AB, Del Campillo E, Catala C, Hayashi T, Henrissat B, Hofte H, McQueen-Mason SJ, Patterson SE, Shoseyov O, Teeri TT, Rose JK (2007) Structural organization and a standardized nomenclature for plant endo-1,4-β-glucanases (cellulases) of glycosyl hydrolase family 9. Plant Physiol 144:1693–1696. https://doi.org/10.1104/pp.107.102574
Veggiani G, Nakamura T, Brenner MD, Gayet RV, Yan J, Robinson CV, Howarth M (2016) Programmable polyproteams built using twin peptide superglues. Proc Natl Acad Sci USA 113:1202–1207. https://doi.org/10.1073/pnas.1519214113
Vina-Gonzalez J, Gonzalez-Perez D, Alcalde M (2016) Directed evolution method in Saccharomyces cerevisiae: mutant library creation and screening. J Vis Exp 110:e53761. https://doi.org/10.3791/53761
Volkov PV, Rubtsova EA, Rozhkova AM, Sinitsyna OA, Zorov IN, Kondratyeva EG, Sinitsyn AP (2021) Properties of recombinant endo-β-1,6-glucanase from Trichoderma harzianum and its application in the pustulan hydrolysis. Carbohydr Res 499:108211. https://doi.org/10.1016/j.carres.2020.108211
Wang J, Wang Y, Wang X, Zhang D, Wu S, Zhang G (2016) Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag/SpyCatcher-mediated spontaneous cyclization. Biotechnol Biofuels 9:79. https://doi.org/10.1186/s13068-016-0490-5
Wang Y, Li D, Dong C, Zhao Y, Zhang L, Yang F, Ye X, Huang Y, Li Z, Cui Z (2021a) Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19. Appl Microbiol Biotechnol 105:6793–6803. https://doi.org/10.1007/s00253-021-11513-6
Wang Y, Zhao Y, Wang X, Zhong L, Fan Q, Lan Z, Ye X, Huang Y, Li Z, Cui Z (2021b) Functional characterization of the novel laminaripentaose-producing β-1,3-glucanase MoGluB and its biocontrol of Magnaporthe oryzae. J Agric Food Chem 69:9571–9584. https://doi.org/10.1021/acs.jafc.1c03072
Wang H, Qi X, Gao S, Zhang Y, An Y (2022) Biochemical characterization of an engineered bifunctional xylanase/feruloyl esterase and its synergistic effects with cellulase on lignocellulose hydrolysis. Bioresour Technol 355:127244. https://doi.org/10.1016/j.biortech.2022.127244
Watanabe M, Matsuzawa T, Yaoi K (2018) Rational protein design for thermostabilization of glycoside hydrolases based on structural analysis. Appl Microbiol Biotechnol 102:8677–8684. https://doi.org/10.1007/s00253-018-9288-7
Westereng B, Kracun SK, Leivers S, Arntzen MO, Aachmann FL, Eijsink VGH (2020) Synthesis of glycoconjugates utilizing the regioselectivity of a lytic polysaccharide monooxygenase. Sci Rep 10:13197. https://doi.org/10.1038/s41598-020-69951-7
Zakeri B, Fierer JO, Celik E, Chittock EC, Schwarz-Linek U, Moy VT, Howarth M (2012) Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci USA 109:E690–697. https://doi.org/10.1073/pnas.1115485109
Zhang YH, Lynd LR (2004) Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol Bioeng 88:797–824. https://doi.org/10.1002/bit.20282
Zhang W, Zhang Y, Lu Y, Herman RA, Zhang S, Hu Y, Zhao W, Wang J, You S (2023) More efficient barley malting under catalyst: thermostability improvement of a β-1,3-1,4-glucanase through surface charge engineering with higher activity. Enzyme Microb Technol 162:110151. https://doi.org/10.1016/j.enzmictec.2022.110151
Zhao J, Shi D, Yang S, Lin H, Chen H (2020) Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity. Appl Microbiol Biotechnol 104:8367–8380. https://doi.org/10.1007/s00253-020-10840-4
Zhou Y, Wang X, Wei W, Xu J, Wang W, Xie Z, Zhang Z, Jiang H, Wang Q, Wei C (2016) A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities. Biotechnol Biofuels 9:36. https://doi.org/10.1186/s13068-016-0449-6
Zhou YB, Cao JW, Sun XB, Wang H, Gao DY, Li YN, Wu KY, Wang JK, Qian GY, Wang Q (2020) Enhanced stability of a rumen-derived xylanase using SpyTag/SpyCatcher cyclization. World J Microbiol Biotechnol 36:33. https://doi.org/10.1007/s11274-020-2809-4
Funding
This work was supported by the Key R & D Program of Zhejiang Province (2022C02043), and National Key Research and Development Program of China (2018YFD0501903).
Author information
Authors and Affiliations
Contributions
XJ was involved in the research and preparation of the original draft of the manuscript. JKW and QW supervised the study and were involved in funding acquisition. Additionally, QW reviewed and edited the manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Additional information
Publisher’s Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Jin, X., Wang, JK. & Wang, Q. Microbial β-glucanases: production, properties, and engineering. World J Microbiol Biotechnol 39, 106 (2023). https://doi.org/10.1007/s11274-023-03550-2
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s11274-023-03550-2