These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Cyclodextrin glycosyltransferases from Klebsiella pneumoniae M 5 al and Bacillus macerans: quantitative analysis by high-performance liquid chromatography of the (1 leads to 4)-alpha-D-glucopyranosyl transfer-products from some linear and cyclic substrates.
    Author: Bender H.
    Journal: Carbohydr Res; 1983 Jun 16; 117():1-11. PubMed ID: 6224557.
    Abstract:
    The analysis of the (1 leads to 4)-alpha-D-glucopyranosyl transfer-products from some linear and cyclic substrates by quantitative h.p.l.c. illuminated the mode of action of the cyclodextrin glycosyltransferases [1 leads to 4)-alpha-D-glucan:[(1 leads to 4)-alpha-D-glucopyranosyl]transferase (cyclising), EC 2.4.1.19) from Klebsiella pneumoniae M 5 al and Bacillus macerans. D-Glucopyranosyl transfer, obligatory for maltose (poor substrate), was preferred for maltotriose (good substrate). The lengths of linear disproportionation-products increased with the lengths of the linear substrates. Cyclodextrins were produced from maltotriose and maltopentaose, but not from maltose. The cyclodextrins were substrates in the absence of acceptors. The cyclodextrin transformation started without the formation of detectable amounts of linear transfer-products. The cyclodextrin composition of long-term digests was nearly the same with all the cyclic substrates, cycloheptaamylose being the main cyclic compound. The linear carbohydrate was uniformly distributed from maltose up to at least maltononaose. The enzyme from Bacillus macerans was the least active, but long-term digests yielded results comparable to those obtained with the enzyme from Klebsiella pneumoniae M 5 al.
    [Abstract] [Full Text] [Related] [New Search]