@article { ISI:000184063400002,
	title = {Enzymatic synthesis of 4-methylumbelliferyl (1 -> 3)-beta-D-glucooligosaccharides - new substrates for beta-1,3-1,4-D-glucanase},
	journal = {CARBOHYDRATE RESEARCH},
	volume = {338},
	number = {14},
	year = {2003},
	month = {JUL 4},
	pages = {1455-1467},
	type = {Article},
	abstract = {The transglycosylation reactions catalyzed by beta-1,3-D-glucanases (laminaranases) were used to synthesize a number of 4-methylumbelliferyl (MeUmb) (1 {\textendash}> 3)-beta-D-gluco-oligosaccharides having the common structure {[}beta-D-Glcp-(1 {\textendash}> 3)](n)-beta-D-Glcp-MeUmb, where n = 1-5. The beta-1,3-D-glucanases used were purified from the culture liquid of Oerskovia sp. and from a homogenate of the marine mollusc Spisula sachalinensis. Laminaran and curdlan were used as (1 {\textendash}> 3)-beta-D-glucan donor substrates, while MeUmb-beta-D-glucoside (MeUmbGlcp) was employed as a transglycosylation acceptor. Modification of {[}beta-D-Glcp-(1 {\textendash}> 3)](2)-beta-D-Glcp-MeUmb (MeUmbG(3)) gives 4,6-O-benzylidene-D-glucopyranosyl or 4,6-O-ethylidene-D-glucopyranosyl groups at the non-reducing end of artificial oligosaccharides. The structures of all oligosaccharides obtained were solved by H-1 and C-13 NMR spectroscopy and electrospray tandem mass spectrometry. The synthetic oligosaccharides were shown to be substrates for a beta-1,3-1,4-D-glucanase from Rhodothermus marinus, which releases MeUmb from beta-di- and beta-triglucosides and from acetal-protected beta-triglucosides. When acting upon substrates with d.p. > 3, the enzyme exhibits an endolytic activity, primarily cleaving off MeUrnbGlcP and MeUmbG(2). (C) 2003 Elsevier Science Ltd. All rights reserved.},
	issn = {0008-6215},
	doi = {10.1016/S0008-6215(03)00199-X},
	author = {Borriss, R and Krah, M and Brumer, H and Kerzhner, MA and Ivanen, DR and Eneyskaya, EV and Elyakova, LA and Shishlyannikov, SM and Shabalin, KA and Neustroev, KN}
}
