Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation

1976 ◽  
Vol 70 (1) ◽  
pp. 8-14 ◽  
Author(s):  
Jeanin Schnapp ◽  
Yechiel Shalitin
Keyword(s):  
Cyanogen Bromide ◽  
Covalent Binding ◽  
Immobilization Of Enzymes ◽  
Cyanogen Bromide Activation

Protein Immobilization in Metal–Organic Frameworks by Covalent Binding

2014 ◽  
Vol 67 (11) ◽  
pp. 1629 ◽  
Author(s):  
Xuan Wang ◽  
Trevor A. Makal ◽  
Hong-Cai Zhou
Keyword(s):  
Enzymatic Activity ◽  
Enzyme Immobilization ◽  
Working Conditions ◽  
Active Site ◽  
Covalent Binding ◽  
Metal Organic Frameworks ◽  
Protein Immobilization ◽  
Immobilization Of Enzymes ◽  
Metal Organic ◽  
Biological Catalysis

Metal–organic frameworks (MOFs), possessing a well defined system of pores, demonstrate extensive potential serving as a platform in biological catalysis. Successful immobilization of enzymes in a MOF system retains the enzymatic activity, renders the active site more accessible to the substrate, and promises recyclability for reuse, and solvent adaptability in a broad range of working conditions. This highlight describes enzyme immobilization on MOFs via covalent binding and its significance.

scholarly journals An Alternative Coupling Procedure for Preparing Activated Sepharose for Affinity Chromatography of Penicillinase

1976 ◽  
Vol 29 (4) ◽  
pp. 305 ◽  
Author(s):  
RG Coombe ◽  
AM George
Keyword(s):  
Affinity Chromatography ◽  
Room Temperature ◽  
Cyanogen Bromide ◽  
Dry Weight ◽  
Enzymic Activity ◽  
Covalent Attachment ◽  
Affinity Column ◽  
Coupling Procedure ◽  
Coupling Techniques ◽  
Cyanogen Bromide Activation

Most applications of affinity chromatography employ the cyanogen bromide activation scheme first devised by Axtm et al. (1967). Porath and Sundberg (1972) reported an alternative procedure in which phloroglucinol and divinylsulphone are used in activating reactions. The advantages of this scheme and parameters relevant to the activating reactions are reported here. Conditions for the attachment of various ligand molecules to sepharose using a divinylsulphone activation method are defined, and a comparison with cyanogen bromide activating and coupling techniques is drawn. a-Chymotrypsin is immobilized by covalent attachment to activated sepharose. The optimum coupling pH is 8� 0-8� 6 and the reaction is virtually complete after 20 h at room temperature. Conjugates containing as much as 2 g of enzyme per gram dry weight of polymer were obtained. The immobilized enzyme retained 41 % of the free enzymic activity. An affinity column of divinylsulphone-activated methicillin-sepharose was used to demonstrate the reversible adsorption of penicillinase.

Improved method for the cyanogen bromide activation of agarose beads

1979 ◽  
Vol 172 (1) ◽  
pp. 221-226 ◽  
Author(s):  
Gunther Kümel ◽  
Heiner Daus ◽  
Harald Mauch
Keyword(s):  
Cyanogen Bromide ◽  
Improved Method ◽  
Agarose Beads ◽  
Cyanogen Bromide Activation

Cyanogen bromide activation of polysaccharides

1977 ◽  
Vol 79 (1-2) ◽  
pp. 513-525 ◽  
Author(s):  
Ronald L. Schnaar ◽  
T.Flint Sparks ◽  
Saul Roseman
Keyword(s):  
Cyanogen Bromide ◽  
Cyanogen Bromide Activation

scholarly journals A study of the mechanism of cyanogen bromide activation of cellulose

1972 ◽  
Vol 14 (6) ◽  
pp. 1039-1044 ◽  
Author(s):  
G. J. Bartling ◽  
H. D. Brown ◽  
L. J. Forrester ◽  
M. T. Koes ◽  
A. N. Mather ◽  
...  
Keyword(s):  
Cyanogen Bromide ◽  
Cyanogen Bromide Activation

Alpha- and beta-amylase immobilized by a covalent binding to hydroxyalkyl methacrylate gels

1980 ◽  
Vol 45 (2) ◽  
pp. 617-622 ◽  
Author(s):  
Karol Babor ◽  
Lubomíra Rexová-Benková
Keyword(s):  
Cyanogen Bromide ◽  
Covalent Binding ◽  
Amylolytic Activity ◽  
Ph Optimum ◽  
Active Preparation

Insoluble active preparation of alpha- and beta-amylase were prepared by a covalent binding of enzymes to hydroxyalkyl methacrylate gel (various kinds of Spheron type) activated with cyanogen bromide. The amount of the bound enzyme, its amylolytic activity on individual substrates, storage and heat stabilities, and pH-optimum were determined.

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