Novel Cell–Inorganic Hybrid Catalytic Interfaces with Enhanced Enzymatic Activity and Stability for Sensitive Biosensing of Paraoxon

2017 ◽  
Vol 9 (8) ◽  
pp. 6894-6901 ◽  
Author(s):  
Lei Han ◽  
Aihua Liu
Keyword(s):  
Enzymatic Activity ◽  
Inorganic Hybrid ◽  
Catalytic Interfaces

Organic−Inorganic Hybrid Silica Monolith Based Immobilized Trypsin Reactor with High Enzymatic Activity

2008 ◽  
Vol 80 (8) ◽  
pp. 2949-2956 ◽  
Author(s):  
Junfeng Ma ◽  
Zhen Liang ◽  
Xiaoqiang Qiao ◽  
Qiliang Deng ◽  
Dingyin Tao ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Inorganic Hybrid ◽  
Silica Monolith ◽  
Hybrid Silica ◽  
Immobilized Trypsin ◽  
High Enzymatic Activity

Facile synthesis of enzyme–inorganic hybrid nanoflowers and their application as an immobilized trypsin reactor for highly efficient protein digestion

RSC Advances ◽  
2014 ◽  
Vol 4 (27) ◽  
pp. 13888-13891 ◽  
Author(s):  
Zian Lin ◽  
Yun Xiao ◽  
Ling Wang ◽  
Yuqing Yin ◽  
Jiangnan Zheng ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Immobilized Enzyme ◽  
Protein Digestion ◽  
Enzyme Reactor ◽  
Facile Synthesis ◽  
Inorganic Hybrid ◽  
Immobilized Enzyme Reactor ◽  
Highly Efficient ◽  
Novel Approach ◽  
Immobilized Trypsin

Hybrid nanoflowers were synthesized by a novel approach. The nanoflowers exhibited an enhanced enzymatic activity and can be used as an immobilized enzyme reactor (IMER) for highly efficient protein digestion.

The influence of synthesis conditions on enzymatic activity of enzyme-inorganic hybrid nanoflowers

2016 ◽  
Vol 133 ◽  
pp. 92-97 ◽  
Author(s):  
Yue Li ◽  
Xu Fei ◽  
Liwen Liang ◽  
Jing Tian ◽  
Longquan Xu ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Inorganic Hybrid ◽  
Synthesis Conditions

An enzyme–inorganic hybrid nanoflower based immobilized enzyme reactor with enhanced enzymatic activity

2015 ◽  
Vol 3 (11) ◽  
pp. 2295-2300 ◽  
Author(s):  
Yuqing Yin ◽  
Yun Xiao ◽  
Guo Lin ◽  
Qi Xiao ◽  
Zian Lin ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Immobilized Enzyme ◽  
Protein Digestion ◽  
Enzyme Reactor ◽  
Inorganic Hybrid ◽  
Immobilized Enzyme Reactor ◽  
Highly Efficient

Ca3(PO4)2–ChT hybrid nanoflowers were synthesized by a facile approach. The nanoflowers exhibited an enhanced enzymatic activity and can be used as an immobilized enzyme reactor (IMER) for highly efficient protein digestion.

Multiscale immobilized lipase for rapid separation and continuous catalysis

2018 ◽  
Vol 42 (16) ◽  
pp. 13471-13478 ◽  
Author(s):  
Weifan Ren ◽  
Xu Fei ◽  
Jing Tian ◽  
Yao Li ◽  
Muzi Jing ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Surface Area ◽  
Enzyme Immobilization ◽  
Chemical Stability ◽  
Immobilized Lipase ◽  
High Surface ◽  
High Surface Area ◽  
Rapid Separation ◽  
Inorganic Hybrid ◽  
Excellent Chemical

Enzyme–inorganic hybrid nanoflowers have drawn extensive research interest for enzyme immobilization owing to their enhanced enzymatic activity, high surface area, and excellent chemical stability.

A Method for the Colorimetric Determination of β-Glucuronidase in Urine, Serum, Tissue; Assay of Enzymatic Activity in Health and Disease

1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg
Keyword(s):  
Enzymatic Activity ◽  
Colorimetric Determination ◽  
Health And Disease ◽  
Urine Serum

Isolation of Antithrombin III from Normal and α1-Antitrypsin-Deficient Human Plasma

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Antithrombin Activity ◽  
Bovine Trypsin ◽  
Normal Plasma ◽  
Antitrypsin Deficiency ◽  
Simplified Procedure ◽  
Stimulation Of

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.

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