𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Substrate-Binding Site of Endo-1,4-β-Xylanase of the Yeast Cryptococcus albidus

✍ Scribed by Peter BIELY; Zdeněk KRÁTKÝ; Mária VRŠANSKÁ


Book ID
115120351
Publisher
John Wiley and Sons
Year
1981
Tongue
English
Weight
573 KB
Volume
119
Category
Article
ISSN
1432-1327

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Xylosyl transfer to cellobiose catalysed
✍ Peter Biely; Mária Vršanská 📂 Article 📅 1983 🏛 Elsevier Science 🌐 English ⚖ 614 KB

In transglycosylation reactions catalysed by an endo-(l-4)P-D-xylanase of the yeast Crypkxoccus albidus, cellobiose is a relatively good acceptor of xylosyl residues. Three transfer products isolated from a reaction mixture containing phenyl P-D-xylopyranoside, cellobiose, and the enzyme were establ

Hydrolysis of (1→3)- and (1→2)-β-d-xylos
✍ Mária Vršanská; Ján Hirsch; Pavol Kováč; Peter Biely 📂 Article 📅 1990 🏛 Elsevier Science 🌐 English ⚖ 494 KB

The substrate specificity of an endo-(1----4)-beta-D-xylanase of the yeast Cryptococcus albidus was investigated using a series of methyl beta-D-xylotriosides. In addition to (1----4) linkages, the enzyme could cleave (1----3) and (1----2) linkages adjacent to a (1----4) linkage and further from the

Soluble chromogenic substrates for the a
✍ Peter Biely; Danica Mislovičová; Rudolf Toman 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 430 KB

New soluble chromogenic substrates were prepared for specific and rapid assays of endo-l,4-/3-xylanases and endo-1 ,4+glucanases. A soluble beechwood 4-0-methyl-D-glucurono-D-xylan was dyed with Remazol brilliant blue R, and hydroxyethylcellulos was coupled to Ostazin brilliant red H-3B. The assays