Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology letters 21 (1999), S. 595-599 
    ISSN: 1573-6776
    Keywords: α-chymotrypsin ; enzyme stability ; glycosylated enzymes ; kyotorphin ; peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract α-Chymotrypsin was covalently modified with cellobiose by chemical means. After adsorption on to a porous polyamide support, both the native and the glycosylated immobilized derivatives were used to synthesize a kyotorphin derivative (N-benzoyl-l-tyrosyl-l-argininamide) in acetonitrile/water. Glycosylated chymotrypsin gave a 125% increase in product formation (750 nmol mg−1 catalyst in 3 h) at 60% (v/v) acetonitrile/water. Maximal protective effect of this glycosylation process was at 70% (v/v) acetonitrile/water, at which concentration the half-life of the glycosylated enzyme was 20-times longer than that of the native form (52 min and 2.8 min, respectively).
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1573-6776
    Keywords: α-chymotrypsin ; dynamic membrane ; enzyme reactor ; peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract α-Chymotrypsin was covalently attached to an α-alumina ultrafiltration membrane coated with an inert protein. This derivative was used as catalyst for the continuous kinetically controlled synthesis of kyotorphin in both membrane and packed bed reactors, using aqueous (water/dimethyl sulfoxide, 60:40, v/v) and nearly-dry (hexane/ethanol/water, 57:40:3, by vol.) organic media, respectively. In both media, the synthetic activity and operational stability of the enzyme-membrane derivative was compared with an adsorbed α-chymotrypsin Celite derivative, being 2-times and 4-times respectively, higher than the Celite one. The enzyme-membrane derivative showed half-life times higher than 36 days, with a selectivity near to 100%.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...