5996-00-9Relevant articles and documents
Properties of recombinant endo-β-1,6-glucanase from Trichoderma harzianum and its application in the pustulan hydrolysis
Volkov,Rubtsova,Rozhkova,Sinitsyna,Zorov,Kondratyeva,Sinitsyn
supporting information, (2020/12/13)
The gene encoding Trichoderma harzianum fungus pustulanase (ThBGL1.6, GH5 family, endo-β-1,6-glucanase, EC 3.2.1.75) was cloned and heterologously expressed by the highly productive Penicillium verruculosum fungus. The recombinant ThBGL1.6 was purified an
Mode of action of a β-(1→6)-glucanase from Penicillium multicolor
Hattori, Takeshi,Kato, Yasuna,Uno, Shuji,Usui, Taichi
, p. 6 - 16 (2013/02/25)
β-(1→6)-Glucanase from the culture filtrate of Penicillium multicolor LAM7153 was purified by ammonium sulfate precipitation, followed by cation-exchange and affinity chromatography using gentiotetraose (Gen 4) as ligand. The hydrolytic mode of action of the purified protein on β-(1→6)-glucan (pustulan) was elucidated in real time during the reaction by HPAEC-PAD analysis. Gentiooligosaccharides (DP 2-9, Gen 2-9), methyl β-gentiooligosides (DP 2-6, Gen2-6 β-OMe), and p-nitrophenyl β-gentiooligosides (DP 2-6, Gen 2-6 β-pNP) were used as substrates to provide analytical insight into how the cleavage of pustulan (DP? 320) is actually achieved by the enzyme. The enzyme was shown to completely hydrolyze pustulan in three steps as follows. In the initial stage, the enzyme quickly cleaved the glucan with a pattern resembling an endo-hydrolase to produce a short-chain glucan (DP? 45) as an intermediate. In the midterm stage, the resulting short-chain glucan was further cleaved into two fractions corresponding to DP 15-7 and DP 2-4 with great regularity. In the final stage, the lower oligomers corresponding to DP 3 and DP 4 were very slowly hydrolyzed into glucose and gentiobiose (Gen 2). As a result, the hydrolytic cooperation of both an endo-type and saccharifying-type reaction by a single enzyme, which plays a bifunctional role, led to complete hydrolysis of the glucan. Thus, β-(1→6)-glucanase varies its mode of action depending on the chain length derived from the glucan.
Identification of oligosaccharides formed during stachyose hydrolysis by pectinex ultra SP-L
Montilla, Antonia,Corzo, Nieves,Olano, Agustin,Jimen, Maria Luisa
experimental part, p. 5007 - 5013 (2010/06/14)
The commercial enzyme preparation Pectinex Ultra SP-L containing fructosyltransferase activity was used to hydrolyze stachyose. During this reaction, besides the formation of mono-, di-, and trisaccharides (DP 3), the presence of one pentasacch
