Immobilization of enzymes masks their active site

1984 ◽  
Vol 4 (3) ◽  
pp. 181-187 ◽  
Author(s):  
Minoru Kumakura ◽  
Isao Kaetsu
Keyword(s):  
Enzyme Activity ◽  
Polymer Matrix ◽  
Active Site ◽  
Immobilized Enzyme ◽  
Monomer Concentration ◽  
Radiation Polymerization ◽  
Immobilization Of Enzymes ◽  
Repeated Batch

We studied the effect of immobilizing cellulase to carboxycellulose sodium by radiation polymerization on the masking of the active site of the enzyme. Masking of the enzyme during the preparation of immobilized enzyme was assayed at tow temperature. The activity of immobilized enzyme was retained during repeated batch reactions, indicating that the enzyme was firmly trapped in the polymer matrix. Various compounds (designated monomers) were used to dissolve the carboxymethylcellulose; enzyme activity was affected by the nature of the monomer, by the monomer concentration, and by the solubility of the substrate in monomer.

Effect of the hydrophilicity of the polymer matrix on immobilized α-chymotrypsin

1984 ◽  
Vol 49 (6) ◽  
pp. 1552-1556
Author(s):  
Minoru Kumakura ◽  
Isso Kaetsu
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Pore Size ◽  
Polymer Matrix ◽  
Low Temperatures ◽  
Radiation Polymerization ◽  
Thermal Stability Of

α-Chymotrypsin was immobilized by radiation polymerization at low temperatures and the effect of the hydrophilicity of the polymer matrix on the enzyme activity and thermal stability was studied. The activity and thermal stability of immobilized chymotrypsin increased with the increasing hydrophilicity of the polymer matrix or monomer. The thermal stability was affected by the form and pore size of the polymer matrix; chymotrypsin immobilized on a soft-gel polymer matrix exhibited an enhanced thermal stability.

scholarly journals N-Acetylglucosamine Production by Repeated-Batch Fermentation Using Immobilized Semi-Purified Chitinase Enzyme on Agar

REAKTOR ◽  
2021 ◽  
Vol 21 (1) ◽  
pp. 11-14
Author(s):  
Lucia Soedirga ◽  
Hardoko Hardoko ◽  
Natasha V Widianto
Keyword(s):  
Enzyme Activity ◽  
Batch Fermentation ◽  
Immobilized Enzyme ◽  
The Third ◽  
Repeated Batch Fermentation ◽  
Chitin Hydrolysis ◽  
Repeated Batch ◽  
Multiple Cycles ◽  
The Stability

Chitinolytic mold, such as Mucor circinelloidesis can be utilized to produce chitinase enzyme for shrimp shell’s chitin hydrolysis into N-acetylglucosamine (NAG). For that purpose, entrapment of chitinase on agar as a carrier could be an alternative way to improve NAG production. This study aimed to investigate the stability of immobilized semi-purified chitinase on agar for multiple cycles fermentation to produce NAG. In this study, 0.6 mL of semi-purified chitinase enzyme was immobilized into 3% of agar matrices and tested for four fermentation cycles to obtain highest NAG concentration and good enzyme activity. The results indicate that the immobilized chitinase could be used for 6 hours fermentation or three fermentation cycles. The NAG concentration produced after three cycle were 1042.22 ± 16.20 ppm. Besides, the immobilized enzyme was considerably stable up to the third cycles with activity value of about 4.74 U/mL.Keywords: agar; immobilized;NAG; repeated fermentation

scholarly journals Effects of morphology and pore size of mesoporous silicas on the efficiency of an immobilized enzyme

RSC Advances ◽  
2021 ◽  
Vol 11 (17) ◽  
pp. 10010-10017
Author(s):  
Ping-Chung Kuo ◽  
Zhi-Xun Lin ◽  
Tzi-Yi Wu ◽  
Chun-Han Hsu ◽  
Hong-Ping Lin ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Mesoporous Silica ◽  
Pore Size ◽  
Immobilized Enzyme ◽  
Mesoporous Silicas ◽  
High Loading ◽  
Loading Capacity ◽  
Silica Films

Mesoporous silica films were used as supports with high loading capacity and enzyme activity.

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.

Immobilization of Enzymes by Radiation Polymerization

1975 ◽  
pp. 185-197 ◽  
Author(s):  
Hideo Suzuki ◽  
Hidekatsu Maeda ◽  
Aizo Yamauchi
Keyword(s):  
Radiation Polymerization ◽  
Immobilization Of Enzymes

scholarly journals Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate

1991 ◽  
Vol 275 (2) ◽  
pp. 349-353 ◽  
Author(s):  
H C Hawkins ◽  
E C Blackburn ◽  
R B Freedman
Keyword(s):  
Enzyme Activity ◽  
Active Site ◽  
Specific Activity ◽  
Disulphide Bond ◽  
Protein Disulphide Isomerase ◽  
Protein Substrate ◽  
Catalytic Domains ◽  
Standard Assay

1. The activities of protein disulphide-isomerase (PDI) and thioredoxin in catalysing disulphide bond isomerization in a protein substrate were compared by using the standard assay, namely the re-activation of ‘scrambled’ RNAase. 2. The specific activity of PDI was 25-fold greater than that of thioredoxin. 3. The greater efficiency of PDI compared with thioredoxin is considered to be due more to the presence of multiple catalytic domains in PDI than to differences in their active-site sequences. 4. Data and procedures were defined for expressing enzyme activity in standard units, i.e. mumol of active RNAase generated/min.

scholarly journals Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity

Structure ◽  
2015 ◽  
Vol 23 (12) ◽  
pp. 2256-2266 ◽  
Author(s):  
Donald Gagné ◽  
Rachel L. French ◽  
Chitra Narayanan ◽  
Miljan Simonović ◽  
Pratul K. Agarwal ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Active Site ◽  
Conformational Dynamics

Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies

2007 ◽  
Vol 63 (8) ◽  
pp. 923-925 ◽  
Author(s):  
Guillaume Poncet-Montange ◽  
Stephanie Ducasse-Cabanot ◽  
Annaick Quemard ◽  
Gilles Labesse ◽  
Martin Cohen-Gonsaud
Keyword(s):  
Enzyme Activity ◽  
Drug Design ◽  
Active Site ◽  
Design Studies
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