Abstract
β-N-Acetylglucosaminidases (GlcNAcases) hydrolyse N-acetylglucosamine-containing oligosaccharides and proteins. These enzymes produce N-acetylglucosamine (GlcNAc) and have a wide range of promising applications in the food, energy, and pharmaceutical industries, such as synergistic degradation of chitin with endo-chitinases and using GlcNAc to produce sialic acid, bioethanol, single-cell proteins, and pharmaceutical therapeutics. GlcNAcases also play an important role in the dynamic balance of cellular O-linked GlcNAc levels, catabolism of ganglioside storage in Tay–Sachs disease, and bacterial cell wall recycling and flagellar assembly. In view of these important biological functions and the wide range of industrial applications of GlcNAcases, this review aims to provide a better understanding of various advances for these enzymes. It focuses on enzymatic properties of GlcNAcases, including substrate specificity, catalytic activity, pH optimum, temperature optimum, thermostability, the effects of various metal ions and organic reagents, and transglycosylation.
Similar content being viewed by others
References
Arnold FH, Wintrode PL, Miyazaki K, Gershenson A (2001) How enzymes adapt: lessons from directed evolution. Trends Biochem Sci 26(2):100–106. https://doi.org/10.1016/S0968-0004(00)01755-2
Bhabha G, Lee J, Ekiert DC, Gam J, Wilson IA, Dyson HJ, Benkovic SJ, Wright PE (2011) A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science 332(6026):234–238. https://doi.org/10.1126/science.1198542
Bruce AF, Gounaris K (2006) Characterisation of a secreted N-acetyl-β-hexosaminidase from Trichinella spiralis. Mol Biochem Parasit 145(1):84–93. https://doi.org/10.1016/j.molbiopara.2005.09.010
Chen F, Chen XZ, Qin LN, Tao Y, Dong ZY (2015) Characterization and homologous overexpression of an N-acetylglucosaminidase Nag1 from Trichoderma reesei. Biochem Biophys Res Commun 459(2):184–188. https://doi.org/10.1016/j.bbrc.2014.12.066
Chen XD, Xu L, Jin L, Sun B, GF G, Lu LL, Xiao M (2016) Efficient and regioselective synthesis of β-GalNAc/GlcNAc-lactose by a bifunctional transglycosylating β-N-acetylhexosaminidase from Bifidobacterium bifidum. Appl Environ Microbiol 82(18):5642–5652. https://doi.org/10.1128/AEM.01325-16
Chitlaru E, Roseman S (1996) Molecular cloning and characterization of a novel β-N-acetyl-D-glucosaminidase from Vibrio furnissii. J Biol Chem 271(52):33433–33439. https://doi.org/10.1074/jbc.271.52.33433
Choi KH, Seo JY, Park KM, Park CS, Cha J (2009) Characterization of glycosyl hydrolase family 3 β-N-acetylglucosaminidases from Thermotoga maritima and Thermotoga neapolitana. J Biosci Bioeng 108(6):455–459. https://doi.org/10.1016/j.jbiosc.2009.06.003
Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ (2006) Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity. Nat Struct Mol Biol 13(4):365–371. https://doi.org/10.1038/nsmb1079
Dong DLY, Hart GW (1994) Purification and characterization of an O-Glcnac selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol. J Biol Chem 269(30):19321–19330
Feller G, Gerday C (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol 1(3):200–208. https://doi.org/10.1038/nrmicro773
Gao Y, Wells L, Comer FI, Parker GJ, Hart GW (2001) Dynamic O-glycosylation of nuclear and cytosolic proteins—cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain. J Biol Chem 276(13):9838–9845. https://doi.org/10.1074/jbc.M010420200
Goni O, Sanchez-Ballesta MT, Merodio C, Escribano MI (2013) Two cold-induced family 19 glycosyl hydrolases from cherimoya (Annona cherimola) fruit: an antifungal chitinase and a cold-adapted chitinase. Phytochemistry 95:94–104. https://doi.org/10.1016/j.phytochem.2013.07.004
Hamed I, Ozogul F, Regenstein JM (2016) Industrial applications of crustacean by-products (chitin, chitosan, and chitooligosaccharides): a review. Trends Food Sci Technol 48:40–50. https://doi.org/10.1016/j.tifs.2015.11.007
Herlihey FA, Moynihan PJ, Clarke AJ (2014) The essential protein for bacterial flagella formation FlgJ functions as a β-N-acetylglucosaminidase. J Biol Chem 289(45):31029–31042. https://doi.org/10.1074/jbc.M114.603944
Husakova L, Herkommerova-Rajnochova E, Semenuk T, Kuzma M, Rauvolfova J, Prikrylova V, Ettrich R, Plihal O, Bezouska K, Kren V (2003) Enzymatic discrimination of 2-acetamido-2-deoxy-D-mannopyranose-containing disaccharides using β-N-acetylhexosaminidases. Adv Synth Catal 345(67):735–742. https://doi.org/10.1002/adsc.200303002
Inokuma K, Hasunuma T, Kondo A (2016) Ethanol production from N-acetyl-D-glucosamine by Scheffersomyces stipitis strains. AMB Express 6(1):83. https://doi.org/10.1186/s13568-016-0267-z
Kaur S, Dhillon GS (2015) Recent trends in biological extraction of chitin from marine shell wastes: a review. Crit Rev Biotechnol 35(1):44–61. https://doi.org/10.3109/07388551.2013.798256
Keyhani NO, Roseman S (1996) The chitin catabolic cascade in the marine bacterium Vibrio furnissii—molecular cloning, isolation, and characterization of a periplasmic β-N-acetylglucosaminidase. J Biol Chem 271(52):33425–33432. https://doi.org/10.1074/jbc.271.52.33425
Kim JS, Yoon BY, Ahn J, Cha J, Ha NC (2015) Crystal structure of β-N-acetylglucosaminidase CbsA from Thermotoga neapolitana. Biochem Biophys Res Commun 464(3):869–874. https://doi.org/10.1016/j.bbrc.2015.07.053
Kubota T, Miyamoto K, Yasuda M, Inamori Y, Tsujibo H (2004) Molecular characterization of an intracellular β-N-acetylglucosaminidase involved in the chitin degradation system of Streptomyces thermoviolaceus OPC-520. Biosci Biotechnol Biochem 68(6):1306–1314. https://doi.org/10.1271/bbb.68.1306
Lakshmanan T, Loganathan D (2005) Enzymatic synthesis of N-glycoprotein linkage region disaccharide mimetics using β-N-acetylhexosaminidases from Aspergillus oryzae and Vigna radiata. Tetrahedron-Asymmetry 16(1):255–260. https://doi.org/10.1016/j.tetasy.2004.11.016
Lan XQ, Ozawa N, Nishiwaki N, Kodaira R, Okazaki M, Shimosaka M (2004) Purification, cloning, and sequence analysis of β-N-acetylglucosaminidase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9. Biosci Biotechnol Biochem 68(5):1082–1090. https://doi.org/10.1271/bbb.68.1082
Lan XQ, Zhang X, Kodaira R, Zhou Z, Shimosaka M (2008) Gene cloning, expression, and characterization of a second β-N-acetylglucosaminidase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9. Biosci Biotechnol Biochem 72(2):492–498. https://doi.org/10.1271/bbb.70573
Lee JO, Yi JK, Lee SG, Takahashi S, Kim BG (2004) Production of N-acetylneuraminic acid from N-acetylglucosamine and pyruvate using recombinant human renin binding protein and sialic acid aldolase in one pot. Enzyme Microbiol Technol 35(2-3):121–125. https://doi.org/10.1016/j.enzmictec.2003.10.020
Lemieux MJ, Mark BL, Cherney MM, Withers SG, Mahuran DJ, James MNG (2006) Crystallographic structure of human β-hexosaminidase A: interpretation of Tay–Sachs mutations and loss of G(M2) ganglioside hydrolysis. J Mol Biol 359(4):913–929. https://doi.org/10.1016/j.jmb.2006.04.004
Li HZ, Morimoto K, Katagiri N, Kimura T, Sakka K, Lun S, Ohmiya K (2002) A novel β-N-acetylglucosaminidase of Clostridium paraputrificum M-21 with high activity on chitobiose. Appl Microbiol Biotechnol 60:420–427
Li HZ, Morimoto K, Kimura T, Sakka K, Ohmiya K (2003) A new type of β-N-acetylglucosaminidase from hydrogen-producing Clostridium paraputrificum M-21. J Biosci Bioeng 96(3):268–274. https://doi.org/10.1016/S1389-1723(03)80192-5
Li BB, Li H, Lu L, Jiang JY (2017) Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Nat Struct Mol Biol 24(4):362–370. https://doi.org/10.1038/nsmb.3390
Lin H, Xiao X, Zeng X, Wang FP (2006) Expression, characterization and mutagenesis of the gene encoding β-N-acetylglucosaminidase from Aeromonas caviae CB101. Enzyme Microbiol Technol 38(6):765–771. https://doi.org/10.1016/j.enzmictec.2005.08.003
Lipski A, Herve M, Lombard V, Nurizzo D, Mengin-Lecreulx D, Bourne Y, Vincent F (2015) Structural and biochemical characterization of the β-N-acetylglucosaminidase from Thermotoga maritima: toward rationalization of mechanistic knowledge in the GH73 family. Glycobiology 25(3):319–330. https://doi.org/10.1093/glycob/cwu113
Lisboa De Marco JL, Valadares-Inglis MC, Felix CR (2004) Purification and characterization of an N-acetylglucosaminidase produced by a Trichoderma harzianum strain which controls Crinipellis perniciosa. Appl Microbiol Biotechnol 64(1):70–75. https://doi.org/10.1007/s00253-003-1490-5
Litzinger S, Duckworth A, Nitzsche K, Risinger C, Wittmann V, Mayer C (2010a) Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase. J Bacteriol 192(12):3132–3143. https://doi.org/10.1128/JB.01256-09
Litzinger S, Fischer S, Polzer P, Diederichs K, Welte W, Mayer C (2010b) Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J Biol Chem 285(46):35675–35684. https://doi.org/10.1074/jbc.M110.131037
Liu TA, Zhang HT, Liu FY, Wu QY, Shen X, Yang Q (2011) Structural determinants of an insect β-N-acetyl-D-hexosaminidase specialized as a chitinolytic enzyme. J Biol Chem 286(6):4049–4058. https://doi.org/10.1074/jbc.M110.184796
Macauley MS, Whitworth GE, Debowski AW, Chin D, Vocadlo DJ (2005) O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J Biol Chem 280(27):25313–25322. https://doi.org/10.1074/jbc.M413819200
Mark BL, Wasney GA, Salo TJS, Khan AR, Cao ZM, Robbins PW, James MNG, Triggs-Raine BL (1998) Structural and functional characterization of Streptomyces plicatus β-N-acetylhexosaminidase by comparative molecular modeling and site-directed mutagenesis. J Biol Chem 273(31):19618–19624. https://doi.org/10.1074/jbc.273.31.19618
Matsuo Y, Kurita M, Park JK, Tanaka K, Nakagawa T, Kawamukai M, Matsuda H (1999) Purification, characterization and gene analysis of N-acetylglucosaminidase from Enterobacter sp. G-1. Biosci Biotechnol Biochem 63(7):1261–1268. https://doi.org/10.1271/bbb.63.1261
Matsuo I, Kim S, Yamamoto Y, Ajisaka K, Maruyama J, Nakajima H, Kitamoto K (2003) Cloning and overexpression of β-N-acetylglucosaminidase encoding gene nagA from Aspergillus oryzae and enzyme-catalyzed synthesis of human milk oligosaccharide. Biosci Biotechnol Biochem 67(3):646–650. https://doi.org/10.1271/bbb.67.646
Mayer C, Vocadlo DJ, Mah M, Rupitz K, Stoll D, Warren RAJ, Withers SG (2006) Characterization of a β-N-acetylhexosaminidase and a β-N-acetylglucosaminidase/β-glucosidase from Cellulomonas fimi. FEBS J 273(13):2929–2941. https://doi.org/10.1111/j.1742-4658.2006.05308.x
Meekrathok P, Suginta W (2016) Probing the catalytic mechanism of Vibrio harveyi GH20 β-N-acetylglucosaminidase by chemical rescue. PLoS One 11(2):e0149228. https://doi.org/10.1371/journal.pone.0149228
Nieder V, Kutzer M, Kren V, Gallego RG, Kamerling JP, Elling L (2004) Screening and characterization of β-N-acetylhexosaminidases for the synthesis of nucleotide-activated disaccharides. Enzyme Microbiol Technol 34(5):407–414. https://doi.org/10.1016/j.enzmictec.2003.11.017
Nyffenegger C, Nordvang RT, Zeuner B, Lezyk M, Difilippo E, Logtenberg MJ, Schols HA, Meyer AS, Mikkelsen JD (2015) Backbone structures in human milk oligosaccharides: trans-glycosylation by metagenomic β-N-acetylhexosaminidases. Appl Microbiol Biotechnol 99(19):7997–8009. https://doi.org/10.1007/s00253-015-6550-0
O'Connell E, Murray P, Piggott C, Hennequart F, Tuohy M (2008) Purification and characterization of a N-acetylglucosaminidase produced by Talaromyces emersonii during growth on algal fucoidan. J Appl Phycol 20(5):557–565. https://doi.org/10.1007/s10811-007-9291-3
Ogawa M, Kitagawa M, Tanaka H, Ueda K, Watsuji T, Beppu T, Kondo A, Kawachi R, Oku T, Nishio T (2006) A β-N-acetylhexosaminidase from Symbiobacterium thermophilum; gene cloning, overexpression, purification and characterization. Enzyme Microbiol Technol 38(3-4):457–464. https://doi.org/10.1016/j.enzmictec.2005.07.009
Ohishi K, Murase K, Etoh H (1999) Purification and properties of β-N-acetylglucosaminidase from Vibrio alginolyticus H-8. J Biosci Bioeng 88(1):98–99. https://doi.org/10.1016/S1389-1723(99)80183-2
Okada S, Obrien JS (1969) Tay–Sachs disease: generalized absence of a β-D-N-acetylhexosaminidase component. Science 165(3894):698–700. https://doi.org/10.1126/science.165.3894.698
Park JK, Kim WJ, Park YI (2011) Purification and characterization of an exo-type β-N-acetylglucosaminidase from Pseudomonas fluorescens JK-0412. J Appl Microbiol 110(1):277–286. https://doi.org/10.1111/j.1365-2672.2010.04879.x
Park HJ, Yim JH, Park H, Kim D (2016) Characterization of β-N-acetylglucosaminidase from a marine Pseudoalteromonas sp. for application in N-acetyl-glucosamine production. Prep Biochem Biotechnol 46(8):764–771. https://doi.org/10.1080/10826068.2015.1135459
Prakash D, Nawani N, Kapadnis B (2013) Cloning, expression and characterization of thermophilic and alkalophilic N-acetylglucosaminidase from Streptomyces sp. NK52 for the targeted production of N-acetylglucosamine. Proc Natl Acad Sci India Sect B Biol Sci 83:431–437
Rajnochova E, Dvorakova J, Hunkova Z, Kren V (1997) Reverse hydrolysis catalysed by β-N-acetylhexosaminidase from Aspergillus oryzae. Biotechnol Lett 19(9):869–872. https://doi.org/10.1023/A:1018385520155
Riekenberg S, Flockenhaus B, Vahrmann A, Muller MCM, Leippe M, Kiess M, Scholze H (2004) The β-N-acetylhexosaminidase of Entamoeba histolytica is composed of two homologous chains and has been localized to cytoplasmic granules. Mol Biochem Parasitol 138(2):217–225. https://doi.org/10.1016/j.molbiopara.2004.09.003
Rivlin M, Navon G (2016) Glucosamine and N-acetyl glucosamine as new CEST MRI agents for molecular imaging of tumors. Sci Rep 6(1):32648. https://doi.org/10.1038/srep32648
Salvatore S, Heuschkel R, Tomlin S, Davies SE, Edwards S, Walker-Smith JA, French I, Murch SH (2000) A pilot study of N-acetyl glucosamine, a nutritional substrate for glycosaminoglycan synthesis, in paediatric chronic inflammatory bowel disease. Aliment Pharmacol Ther 14:1567–1579
Santiago M, Ramirez-Sarmiento CA, Zamora RA, Parra LP (2016) Discovery, molecular mechanisms, and industrial applications of cold-active enzymes. Front Microbiol 7:1408. https://doi.org/10.3389/fmicb.2016.01408
Senba M, Kashige N, Nakashima K, Miake F, Watanabe K (2000) Cloning of the gene of β-N-acetylglucosaminidase from Lactobacillus casei ATCC 27092 and characterization of the enzyme espressed in Escherichia coli. Biol Pharm Bull 23(5):527–531. https://doi.org/10.1248/bpb.23.527
Sheldon WL, MacAuley MS, Taylor EJ, Robinson CE, Charnock SJ, Davies GJ, Vocadlo DJ, Black GW (2006) Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a β-N-acetylglucosaminidase and not a hyaluronidase. Biochem J 399(2):241–247. https://doi.org/10.1042/BJ20060307
Shikhman AR, Amiel D, D'Lima D, Hwang SB, Hu C, Xu A, Hashimoto S, Kobayashi K, Sasho T, Lotz MK (2005) Chondroprotective activity of N-acetylglucosamine in rabbits with experimental osteoarthritis. Ann Rheum Dis 64(1):89–94. https://doi.org/10.1136/ard.2003.019406
da Silva Junior Sobrinho I, Bataus LAM, Maitan VR, Ulhoa CJ (2005) Purification and properties of an N-acetylglucosaminidase from Streptomyces cerradoensis. Biotechnol Lett 27:1273–1276
Slamova K, Bojarova P, Petraskova L, Kren V (2010) β-N-Acetylhexosaminidase: what’s in a name...? Biotechnol Adv 28(6):682–693. https://doi.org/10.1016/j.biotechadv.2010.04.004
Slamova K, Kulik N, Fiala M, Krejzova-Hofmeisterova J, Ettrich R, Kren V (2014) Expression, characterization and homology modeling of a novel eukaryotic GH84 β-N-acetylglucosaminidase from Penicillium chrysogenum. Protein Expr Purif 95:204–210. https://doi.org/10.1016/j.pep.2014.01.002
Sukprasirt P, Wititsuwannakul R (2014) A chitinolytic endochitinase and β-N-acetylglucosaminidase-based system from Hevea latex in generating N-acetylglucosamine from chitin. Phytochemistry 104:5–11. https://doi.org/10.1016/j.phytochem.2014.04.001
Sumida T, Ishii R, Yanagisawa T, Yokoyama S, Ito M (2009) Molecular cloning and crystal structural analysis of a novel β-N-acetylhexosaminidase from Paenibacillus sp. TS12 capable of degrading glycosphingolipids. J Mol Biol 392(1):87–99. https://doi.org/10.1016/j.jmb.2009.06.025
Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24(8):1596–1599. https://doi.org/10.1093/molbev/msm092
Tews I, Vincentelli R, Vorgias CE (1996) N-Acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli. Gene 170(1):63–67. https://doi.org/10.1016/0378-1119(95)00848-9
Tomiya N, Narang S, Park J, Abdul-Rahman B, Choi O, Singh S, Hiratake J, Sakata K, Betenbaugh MJ, Palter KB, Lee YC (2006) Purification, characterization, and cloning of a Spodoptera frugiperda Sf9 β-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core. J Biol Chem 281(28):19545–19560. https://doi.org/10.1074/jbc.M603312200
Tsujibo H, Fujimoto K, Tanno H, Miyamoto K, Kimura Y, Imada C, Okami Y, Inamori Y (1995) Molecular cloning of the gene which encodes β-N-acetylglucosaminidase from a marine bacterium, Alteromonas sp. strain O-7. Appl Environ Microbiol 61:804–806
Tsujibo H, Hatano N, Mikami T, Hirasawa A, Miyamoto K, Inamori Y (1998a) A novel β-N-acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: gene cloning, expression, and assignment to family 3 of the glycosyl hydrolases. Appl Environ Microbiol 64:2920–2924
Tsujibo H, Hatano N, Mikami T, Izumizawa Y, Miyamoto K, Inamori Y (1998b) Cloning, characterization and expression of β-N-acetylglucosaminidase gene from Streptomyces thermoviolaceus OPC-520. BBA-Gen Subjects 1425(2):437–440. https://doi.org/10.1016/S0304-4165(98)00098-1
Tsujibo H, Miyamoto K, Yoshimura M, Takata M, Miyamoto J, Inamori Y (2002) Molecular cloning of the gene encoding a novel β-N-acetylhexosaminidase from a marine bacterium, Alteromonas sp. strain O-7, and characterization of the cloned enzyme. Biosci Biotechnol Biochem 66(2):471–475. https://doi.org/10.1271/bbb.66.471
Ueda M, Fujita Y, Kawaguchi T, Arai M (2000) Cloning, nucleotide sequence and expression of the β-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24. J Biosci Bioeng 89(2):164–169. https://doi.org/10.1016/S1389-1723(00)88731-9
Votsch W, Templin MF (2000) Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J Biol Chem 275(50):39032–39038. https://doi.org/10.1074/jbc.M004797200
Vyas P, Deshpande M (1991) Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP. J Gen Appl Microbiol 37(3):267–275. https://doi.org/10.2323/jgam.37.267
Wang XH, Chi NY, Bai FW, Du YG, Zhao Y, Yin H (2016) Characterization of a cold-adapted and salt-tolerant exo-chitinase (ChiC) from Pseudoalteromonas sp. DL-6. Extremophiles 20(2):167–176. https://doi.org/10.1007/s00792-016-0810-5
Yang SQ, Song S, Yan QJ, Fu X, Jiang ZQ, Yang XB (2014) Biochemical characterization of the first fungal glycoside hydrolyase family 3 β-N-acetylglucosaminidase from Rhizomucor miehei. J Agric Food Chem 62(22):5181–5190. https://doi.org/10.1021/jf500912b
Yu HR, Huang H (2014) Engineering proteins for thermostability through rigidifying flexible sites. Biotechnol Adv 32:308–315
Zhou JP, Song ZF, Zhang R, Ding LM, Wu Q, Li JJ, Tang XH, Xu B, Ding JM, Han NY, Huang ZX (2016) Characterization of a NaCl-tolerant β-N-acetylglucosaminidase from Sphingobacterium sp. HWLB1. Extremophiles 20(4):547–557. https://doi.org/10.1007/s00792-016-0848-4
Zhou JP, Song ZF, Zhang R, Chen CH, Wu Q, Li JJ, Tang XH, Xu B, Ding JM, Han NY, Huang ZX (2017a) A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics. Extremophiles 21(4):699–709. https://doi.org/10.1007/s00792-017-0935-1
Zhou JP, Song ZF, Zhang R, Liu R, Wu Q, Li JJ, Tang XH, Xu B, Ding JM, Han NY, Huang ZX (2017b) Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance. BMC Biotechnol 17(1):37. https://doi.org/10.1186/s12896-017-0358-1
Funding
This work was supported by the National Key Research and Development Program of China (grant no. 2017YFB0308401), the Yunling Scholars (grant no. 2015 56), the Yunling Industry Leading Talents (grant no. 2014 1782), the Reserve Talents Project for Young and Middle-Aged Academic and Technical Leaders of Yunnan Province (grant no. 2015HB033), and the Applied and Basic Research Foundation of Yunnan Province (grant no. 201401PC00224).
Author information
Authors and Affiliations
Corresponding authors
Ethics declarations
Conflict of interest
The authors declare that they have no competing interests.
Ethical approval
This article does not contain any studies with human participants or animals performed by any of the authors.
Rights and permissions
About this article
Cite this article
Zhang, R., Zhou, J., Song, Z. et al. Enzymatic properties of β-N-acetylglucosaminidases. Appl Microbiol Biotechnol 102, 93–103 (2018). https://doi.org/10.1007/s00253-017-8624-7
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00253-017-8624-7