A new robust bio-inspired route by using lysozyme aqueous solution for surface modification on 1,3,5,7-tetranitro-1,3,5,7-tetrazocane(HMX)was described in this paper.HMX crystals were coated by in situ phase transitio...A new robust bio-inspired route by using lysozyme aqueous solution for surface modification on 1,3,5,7-tetranitro-1,3,5,7-tetrazocane(HMX)was described in this paper.HMX crystals were coated by in situ phase transition of lysozyme(PTL)molecules.The HMX decorated by PTL was characterized by SEM,XRD,FTIR and XPS,demonstrating a dense core-shell coating layer.The coverage of lysozyme on HMX crystal was calculated by the ratio of sulfur content.The surface coverage increased from 60.5% to 93.5% when the content of PTL was changed from 0.5 wt% to 2.0 wt%,indicating efficient coating.The thermal stability of HMX was investigated by in situ XRD and DSC.The thermal phase transition temperature of HMX(β to δ phase)was delayed by 42℃ with 2.0 wt% PTL coating,which prevented HMX from thermal damage and sensitivity by the effect of PTL coating.After heating at 215℃,large cracks appeared in the naked HMX crystal,while the PTL coated HMX still maintained intact,with the impact energy of HMX dropped dramatically from 5 J to 2 J.However,the impact energy of HMX with 1.0 wt% and 2.0 wt% coating content(HMX@PTL-1.0 and HMX@PTL-2.0)was unchanged(5 J).Present results potentially enable large-scale fabrication of polymorphic energetic materials with outstanding thermal stability by novel lysozyme coating.展开更多
The corrosion inhibition performance of co-immobilized lysozyme and lipase was investigated in a recirculating cooling water system. Four methods were carried out in co-immobilization, and the operating parameters wer...The corrosion inhibition performance of co-immobilized lysozyme and lipase was investigated in a recirculating cooling water system. Four methods were carried out in co-immobilization, and the operating parameters were optimized by using the respond surface methodology(RSM). The corrosion inhibition performance of co-immobilized lipase and lysozyme was evaluated by weight loss measurements and electrochemical measurements. The results revealed that the optimal co-immobilization method should be the sequential immobilization of lysozyme and then lipase. The inhibition efficiency was 86.10% under the optimal co-immobilized conditions. Electrochemical data showed that co-immobilized lysozyme and lipase was a mixed-type inhibitor and the corrosion inhibition efficiency was 81%.展开更多
Molecular imprinting technology has a great potential to be used in protein separation and purification. In this work, lysozyme imprinted polyacrylamide gel was prepared with silica particles as a sacrificial template...Molecular imprinting technology has a great potential to be used in protein separation and purification. In this work, lysozyme imprinted polyacrylamide gel was prepared with silica particles as a sacrificial template to generate macro-porosity for fast adsorption. The adsorption equilibrium time and adsorption capacity were 9 h and 56 mg/g respectively, which was 2 h less and 2.3-fold more than polymers without the sacrificial template. In order to test molecular imprinting polymers （MIPs） ＇ selectivity, bovine serum albumin （BSA） was chosen as interferent for binary adsorption tests. In addition, the adsorption selectivity was further investigated using different molar ratios of lysozyme to BSA with fixed total concentration of proteins, as well as using various total concentra- tions of proteins with an equimolar ratio of lysozyme to BSA. It has been proven that the total con- centration of proteins should be larger than 1.5 × 10^-7 mol/mL, when the molar ratio of BSA to Lyz is 1： 1, in order to effectively separate Lyz from the binary protein mixture. The macro-porous lyso- zyme molecularly imprinted polymers have less adsorption time, larger adsorption capacity, and bet- ter imprinting effect.展开更多
In order to improve the stability and corrosion inhibition performance of bioenzyme, lipase and lsozyme were co-immobilized on the mesoporous molecular sieve MCM-41 by the adsorption method. Then the immobilized enzym...In order to improve the stability and corrosion inhibition performance of bioenzyme, lipase and lsozyme were co-immobilized on the mesoporous molecular sieve MCM-41 by the adsorption method. Then the immobilized enzymes were combined with amino trimethylene phosphonic acid and polyaspartic acid to prevent corrosion caused by circulating cooling water. The weight-loss method and electrochemical techniques were used to evaluate the performance of composite inhibitors. The co-immobilized lysozyme and lipase achieved good inhibition effects. After they were combined with amino trimethylene phosphonic acid and polyaspartic acid, the corrosion inhibition properties were further improved. The inhibition efficiency was promoted to 94.4%. During the corrosion inhibition process, the immobilized enzymes played an important role. The addition of corrosion inhibitor could inhibit the anodic dissolution and cathodic hydrogen evolution process of carbon steel at the same time. The adsorption of co-immobilized lysozyme and lipase composite inhibitor on the steel surface was a joint action involving physical adsorption and chemical adsorption.展开更多
The interaction between proteins and lipids is one of the basic problems of modern biochemistry and biophysics.The purpose of this study is to compare the penetration degree of lysozyme into 1,2-diapalmitoyl-sn-glycer...The interaction between proteins and lipids is one of the basic problems of modern biochemistry and biophysics.The purpose of this study is to compare the penetration degree of lysozyme into 1,2-diapalmitoyl-sn-glycero-3-phosphocholine（DPPC） and 1,2-dipalmitoyl-sn-glycero-3-phosphoethano-lamine（DPPE） by analyzing the data of surface pressure–area（π–A） isotherms and surface pressure–time（π–T） curves.Lysozyme can penetrate into both DPPC and DPPE monolayers because of the increase of surface pressure at an initial pressure of 15 m N/m.However,the changes of DPPE are larger than DPPC,indicating stronger interaction of lysozyme with DPPE than DPPC.The reason may be due to the different head groups and phase state of DPPC and DPPE monolayers at the surface pressure of 15 m N/m.Atomic force microscopy reveals that lysozyme was absorbed by DPPC and DPPE monolayers,which leads to self-aggregation and self-assembly,forming irregular multimers and conical multimeric.Through analysis,we think that the process of polymer formation is similar to the aggregation mechanism of amyloid fibers.展开更多
基金the China National Nature Science Foundation(Grant No.12102404)。
文摘A new robust bio-inspired route by using lysozyme aqueous solution for surface modification on 1,3,5,7-tetranitro-1,3,5,7-tetrazocane(HMX)was described in this paper.HMX crystals were coated by in situ phase transition of lysozyme(PTL)molecules.The HMX decorated by PTL was characterized by SEM,XRD,FTIR and XPS,demonstrating a dense core-shell coating layer.The coverage of lysozyme on HMX crystal was calculated by the ratio of sulfur content.The surface coverage increased from 60.5% to 93.5% when the content of PTL was changed from 0.5 wt% to 2.0 wt%,indicating efficient coating.The thermal stability of HMX was investigated by in situ XRD and DSC.The thermal phase transition temperature of HMX(β to δ phase)was delayed by 42℃ with 2.0 wt% PTL coating,which prevented HMX from thermal damage and sensitivity by the effect of PTL coating.After heating at 215℃,large cracks appeared in the naked HMX crystal,while the PTL coated HMX still maintained intact,with the impact energy of HMX dropped dramatically from 5 J to 2 J.However,the impact energy of HMX with 1.0 wt% and 2.0 wt% coating content(HMX@PTL-1.0 and HMX@PTL-2.0)was unchanged(5 J).Present results potentially enable large-scale fabrication of polymorphic energetic materials with outstanding thermal stability by novel lysozyme coating.
基金financially supported by the National Natural Science Foundation of China (project 21077133)the Natural Foundation of Shandong Province and the Top Talent Project of China University of Petroleum (16RC17040003)
文摘The corrosion inhibition performance of co-immobilized lysozyme and lipase was investigated in a recirculating cooling water system. Four methods were carried out in co-immobilization, and the operating parameters were optimized by using the respond surface methodology(RSM). The corrosion inhibition performance of co-immobilized lipase and lysozyme was evaluated by weight loss measurements and electrochemical measurements. The results revealed that the optimal co-immobilization method should be the sequential immobilization of lysozyme and then lipase. The inhibition efficiency was 86.10% under the optimal co-immobilized conditions. Electrochemical data showed that co-immobilized lysozyme and lipase was a mixed-type inhibitor and the corrosion inhibition efficiency was 81%.
文摘Molecular imprinting technology has a great potential to be used in protein separation and purification. In this work, lysozyme imprinted polyacrylamide gel was prepared with silica particles as a sacrificial template to generate macro-porosity for fast adsorption. The adsorption equilibrium time and adsorption capacity were 9 h and 56 mg/g respectively, which was 2 h less and 2.3-fold more than polymers without the sacrificial template. In order to test molecular imprinting polymers （MIPs） ＇ selectivity, bovine serum albumin （BSA） was chosen as interferent for binary adsorption tests. In addition, the adsorption selectivity was further investigated using different molar ratios of lysozyme to BSA with fixed total concentration of proteins, as well as using various total concentra- tions of proteins with an equimolar ratio of lysozyme to BSA. It has been proven that the total con- centration of proteins should be larger than 1.5 × 10^-7 mol/mL, when the molar ratio of BSA to Lyz is 1： 1, in order to effectively separate Lyz from the binary protein mixture. The macro-porous lyso- zyme molecularly imprinted polymers have less adsorption time, larger adsorption capacity, and bet- ter imprinting effect.
基金financially supported by Shandong Natural Science Foundation (ZR201702140013)
文摘In order to improve the stability and corrosion inhibition performance of bioenzyme, lipase and lsozyme were co-immobilized on the mesoporous molecular sieve MCM-41 by the adsorption method. Then the immobilized enzymes were combined with amino trimethylene phosphonic acid and polyaspartic acid to prevent corrosion caused by circulating cooling water. The weight-loss method and electrochemical techniques were used to evaluate the performance of composite inhibitors. The co-immobilized lysozyme and lipase achieved good inhibition effects. After they were combined with amino trimethylene phosphonic acid and polyaspartic acid, the corrosion inhibition properties were further improved. The inhibition efficiency was promoted to 94.4%. During the corrosion inhibition process, the immobilized enzymes played an important role. The addition of corrosion inhibitor could inhibit the anodic dissolution and cathodic hydrogen evolution process of carbon steel at the same time. The adsorption of co-immobilized lysozyme and lipase composite inhibitor on the steel surface was a joint action involving physical adsorption and chemical adsorption.
基金Project supported by the National Natural Science Foundation of China(Grant Nos.21402114 and 11544009)the Natural Science Basic Research Plan in Shaanxi Province of China(Grant No.2016JM2010)+1 种基金the Fundamental Research Funds for the Central Universities of China(Grant No.GK201603026)the National University Science and Technology Innovation Project of China(Grant No.201610718013)
文摘The interaction between proteins and lipids is one of the basic problems of modern biochemistry and biophysics.The purpose of this study is to compare the penetration degree of lysozyme into 1,2-diapalmitoyl-sn-glycero-3-phosphocholine（DPPC） and 1,2-dipalmitoyl-sn-glycero-3-phosphoethano-lamine（DPPE） by analyzing the data of surface pressure–area（π–A） isotherms and surface pressure–time（π–T） curves.Lysozyme can penetrate into both DPPC and DPPE monolayers because of the increase of surface pressure at an initial pressure of 15 m N/m.However,the changes of DPPE are larger than DPPC,indicating stronger interaction of lysozyme with DPPE than DPPC.The reason may be due to the different head groups and phase state of DPPC and DPPE monolayers at the surface pressure of 15 m N/m.Atomic force microscopy reveals that lysozyme was absorbed by DPPC and DPPE monolayers,which leads to self-aggregation and self-assembly,forming irregular multimers and conical multimeric.Through analysis,we think that the process of polymer formation is similar to the aggregation mechanism of amyloid fibers.
