Enzymatic modification of vegetable protein: Immobilization ofPenicillium duponti enzyme on reconstituted collagen and the use of the immobilized-enzyme complex for solubilizing vegetable protein in a recycle reactor

1981 ◽  
Vol 23 (11) ◽  
pp. 2609-2627 ◽  
Author(s):  
B. Adu-Amankwa ◽  
A. Constantinides ◽  
W. R. Vieth
Keyword(s):  
Vegetable Protein ◽  
Immobilized Enzyme ◽  
Protein Immobilization ◽  
Enzyme Complex ◽  
Enzymatic Modification ◽  
Recycle Reactor

scholarly journals Rapid protein immobilization for thin film continuous flow biocatalysis

2016 ◽  
Vol 52 (66) ◽  
pp. 10159-10162 ◽  
Author(s):  
Joshua Britton ◽  
Colin L. Raston ◽  
Gregory A. Weiss
Keyword(s):  
Thin Film ◽  
Enzyme Activity ◽  
Enzyme Immobilization ◽  
Continuous Flow ◽  
Immobilized Enzyme ◽  
Protein Immobilization

Continuous flow biocatalysis gets a new spin. An efficient and general enzyme immobilization technique for vortex fluidic processing has been developed. The immobilized enzyme demonstrated no decrease in enzyme activity over 10 h in continuous flow with a >95% reduction in quantities of required reagents and enzymes.

Accelerated CO2 capture in hybrid solvent using co-immobilized enzyme/complex on a hetero-functionalized support

2017 ◽  
Vol 21 ◽  
pp. 77-81 ◽  
Author(s):  
Prakash C. Sahoo ◽  
Manoj Kumar ◽  
Amardeep Singh ◽  
M.P. Singh ◽  
S.K. Puri ◽  
...  
Keyword(s):  
Co2 Capture ◽  
Immobilized Enzyme ◽  
Enzyme Complex

The performance of mesoporous organosilicas with phenyl groups in Heme protein immobilization

2015 ◽  
Vol 39 (1) ◽  
pp. 739-745 ◽  
Author(s):  
Yu Xiao ◽  
Buyuan Guan ◽  
Xue Wang ◽  
Zhuofu Wu ◽  
Yunling Liu ◽  
...  
Keyword(s):  
Pore Structure ◽  
Immobilized Enzyme ◽  
Protein Immobilization ◽  
Heme Protein ◽  
Mesoporous Organosilicas

We demonstrate the influence of phenyl groups in the pore structure of mesoporous organosilicas, on the quantity of absorbed enzyme and the activity of immobilized enzyme.

Comparing soluble Trametes pubescens laccase and cross-linked enzyme crystals (CLECs) for enzymatic modification of cellulose 10th EWLP, Stockholm, Sweden, August 25–28, 2008

Holzforschung ◽  
2009 ◽  
Vol 63 (6) ◽  
Author(s):  
Ilabahen Patel ◽  
Roland Ludwig ◽  
Kitti Mueangtoom ◽  
Dietmar Haltrich ◽  
Thomas Rosenau ◽  
...  
Keyword(s):  
Immobilized Enzyme ◽  
Enzyme System ◽  
Low Molecular Weight ◽  
Organic Media ◽  
Enzymatic Modification ◽  
Eupergit C ◽  
Enzyme Form ◽  
Highly Active ◽  
Cellulose Substrates ◽  
High Volumetric Productivity

Abstract Three types of preparations – enzyme immobilized on Eupergit C, cross-linked enzyme crystals (CLECs) and lyophilized enzyme – have been obtained from Trametes pubescens laccase. Their activity in organic solvents has been comparatively evaluated, whereby the CLECs showed a significantly higher activity compared to the immobilized and the lyophilized variant. The soluble, lyophilized laccase and the CLECs were compared for their activity in the oxidation of cellulose in the laccase/TEMPO system. The “double heterogeneous” CLEC system – both the CLECs and the cellulose substrates are solids and only the mediator is homogeneously dissolved – showed similar reactivity to the conventional enzyme system. Laccase CLECs, being a solid, robust and highly active immobilized enzyme form can be conveniently used to modify (protected) low-molecular weight carbohydrates or cellulosics also in (aqueous-)organic media, and they offer many practical advantages: operational stability and ease of recycling coupled with high volumetric productivity.

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

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