The Experts below are selected from a list of 33951 Experts worldwide ranked by ideXlab platform
Qiuyu Zhang - One of the best experts on this subject based on the ideXlab platform.
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papain zn3 po4 2 hybrid nanoflower preparation characterization and its enhanced catalytic activity as an Immobilized Enzyme
RSC Advances, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Lili Fan, Qiuyu ZhangAbstract:Flower-like papain/Zn3(PO4)2 hybrid materials are synthesized via a facile, rapid and low-cost method in this study. The growth process of the nanoflowers has been studied in detail and a four-step formation mechanism, including coordination, precipitation, self-assembly and size growth, has been clarified. The concentration of papain mainly affects the morphology of the products by regulating the assembly and crystal growth. The Enzyme activity of papain/Zn3(PO4)2 hybrid nanoflowers, a novel Immobilized Enzyme, was calculated by monitoring the hydrolysis reaction of casein. The results show that the catalytic properties of papain Immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The as-prepared hybrid nanoflowers exhibited excellent reusability, high thermo stability and long storage life. The results indicate that the well-designed materials have great potential in industrial applications.
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preparation of lipase zn3 po4 2 hybrid nanoflower and its catalytic performance as an Immobilized Enzyme
Chemical Engineering Journal, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Qiuyu ZhangAbstract:Abstract A facile and rapid method is reported in this paper to prepare a novel Immobilized Enzyme named lipase/Zn3(PO4)2 hybrid nanoflower. The growth mechanism of the nanoflower has been studied in detail and can be described as the following four steps: crystallization and coordination, in-situ precipitation, self-assembly, size growth. Addition amount of lipase, reaction temperature and stirring form affect the morphology and lipase content of the hybrid nanoflower. Besides, the catalytic performance of lipase/Zn3(PO4)2 hybrid nanoflower was investigated and the optimal catalytic conditions have been found. The maximum Enzyme activity was 855 ± 13 U/g. In comparison with the free lipase, the Enzyme activity increment of hybrid nanoflower is 147%. Meanwhile, the unique nanostructure makes lipase/Zn3(PO4)2 hybrid nanoflower an excellent operational stabilizer. The results indicate that the well-designed materials should be useful in industrial Enzyme catalysis.
Asmita Prabhune - One of the best experts on this subject based on the ideXlab platform.
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hypocholesteremic effect of bile salt hydrolase from lactobacillus buchneri atcc 4005
Food Research International, 2009Co-Authors: N. Sridevi, Pradnya Vishwe, Asmita PrabhuneAbstract:The effect of oral administration of the Immobilized bile salt hydrolase Enzyme on serum cholesterol, triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia was assessed. Culture conditions were optimized for the production of bile salt hydrolase, which resulted in 2.9-fold enhancement in activity. Bile salt hydrolase (BSH; E.C.3.5.1.24) was isolated from Lactobacillus buchneri ATCC 4005 and Immobilized in 0.5% gellan gum gel. The Immobilized Enzyme was orally delivered in wistar rats, induced with hypercholesteremia by triton X-100. The serum cholesterol and triglycerides were reduced by 50% and 15%, respectively, in the group fed with Immobilized Enzyme 10 IU/kg dose whereas administration of 20 IU/kg Immobilized Enzyme resulted in reduction of serum cholesterol by 58% and triglycerides by 45%, respectively. The results indicate that bile salt hydrolase has potential cholesterol lowering property and oral administration of the Immobilized Enzyme is an alternative pharmacological approach to reduce serum cholesterol levels.
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hypocholesteremic effect of bile salt hydrolase from lactobacillus buchneri atcc 4005
Food Research International, 2009Co-Authors: N. Sridevi, Pradnya Vishwe, Asmita PrabhuneAbstract:The effect of oral administration of the Immobilized bile salt hydrolase Enzyme on serum cholesterol, triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia was assessed. Culture conditions were optimized for the production of bile salt hydrolase, which resulted in 2.9-fold enhancement in activity. Bile salt hydrolase (BSH; E.C.3.5.1.24) was isolated from Lactobacillus buchneri ATCC 4005 and Immobilized in 0.5% gellan gum gel. The Immobilized Enzyme was orally delivered in wistar rats, induced with hypercholesteremia by triton X-100. The serum cholesterol and triglycerides were reduced by 50% and 15%, respectively, in the group fed with Immobilized Enzyme 10 IU/kg dose whereas administration of 20 IU/kg Immobilized Enzyme resulted in reduction of serum cholesterol by 58% and triglycerides by 45%, respectively. The results indicate that bile salt hydrolase has potential cholesterol lowering property and oral administration of the Immobilized Enzyme is an alternative pharmacological approach to reduce serum cholesterol levels.
Baoliang Zhang - One of the best experts on this subject based on the ideXlab platform.
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papain zn3 po4 2 hybrid nanoflower preparation characterization and its enhanced catalytic activity as an Immobilized Enzyme
RSC Advances, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Lili Fan, Qiuyu ZhangAbstract:Flower-like papain/Zn3(PO4)2 hybrid materials are synthesized via a facile, rapid and low-cost method in this study. The growth process of the nanoflowers has been studied in detail and a four-step formation mechanism, including coordination, precipitation, self-assembly and size growth, has been clarified. The concentration of papain mainly affects the morphology of the products by regulating the assembly and crystal growth. The Enzyme activity of papain/Zn3(PO4)2 hybrid nanoflowers, a novel Immobilized Enzyme, was calculated by monitoring the hydrolysis reaction of casein. The results show that the catalytic properties of papain Immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The as-prepared hybrid nanoflowers exhibited excellent reusability, high thermo stability and long storage life. The results indicate that the well-designed materials have great potential in industrial applications.
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preparation of lipase zn3 po4 2 hybrid nanoflower and its catalytic performance as an Immobilized Enzyme
Chemical Engineering Journal, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Qiuyu ZhangAbstract:Abstract A facile and rapid method is reported in this paper to prepare a novel Immobilized Enzyme named lipase/Zn3(PO4)2 hybrid nanoflower. The growth mechanism of the nanoflower has been studied in detail and can be described as the following four steps: crystallization and coordination, in-situ precipitation, self-assembly, size growth. Addition amount of lipase, reaction temperature and stirring form affect the morphology and lipase content of the hybrid nanoflower. Besides, the catalytic performance of lipase/Zn3(PO4)2 hybrid nanoflower was investigated and the optimal catalytic conditions have been found. The maximum Enzyme activity was 855 ± 13 U/g. In comparison with the free lipase, the Enzyme activity increment of hybrid nanoflower is 147%. Meanwhile, the unique nanostructure makes lipase/Zn3(PO4)2 hybrid nanoflower an excellent operational stabilizer. The results indicate that the well-designed materials should be useful in industrial Enzyme catalysis.
Mehmet Mutlu - One of the best experts on this subject based on the ideXlab platform.
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immobilization of aspergillus oryzae β galactosidase on low pressure plasma modified cellulose acetate membrane using polyethyleneimine for production of galactooligosaccharide
Biotechnology and Bioprocess Engineering, 2010Co-Authors: Sevim Gurdas, Haci Ali Gulec, Nedim Albayrak, Mehmet MutluAbstract:The aim of this study was to produce galactooligosaccharides (GOS) from lactose using β-galactosidase from Aspergillus oryzae Immobilized on a low-pressure plasma-modified cellulose acetate (CA) membrane. Specifically, a novel method was developed for multilayer Enzyme immobilization involving polyethyleneimine (PEI)-Enzyme aggregate formation and growth on a CA membrane. A large amount of Enzyme (997 μg/cm2 membrane) was Immobilized with 66% efficiency. The K m value for the Immobilized Enzyme was estimated to be 48 mM, which indicates decreased affinity for the substrate, whereas the Vmax value was smaller. The Immobilized Enzyme showed good storage and operational stability. The half-life of the Immobilized Enzyme on the membrane was about 1 month at 30°C and ∼ 60 h at 60°C. Maximum GOS production of 27% (w/w) was achieved with 70% lactose conversion from 320 g/L of lactose at pH 4.5 and 60°C. Trisaccharides were the major types of GOS formed and accounted for about 75% of the total GOS produced. Based on these results, Immobilized Enzyme technology could be applied to GOS production from lactose.
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determination of apparent kinetic parameters for competitive product inhibition in packed bed Immobilized Enzyme reactors
Biochemical Engineering Journal, 2003Co-Authors: Ahmet R Ozdural, Deniz Tanyolac, Mehmet Mutlu, Ismail Hakki Boyaci, Colin WebbAbstract:Abstract In this study, a simple and effective technique for characterizing Michaelis–Menten type kinetics with competitive product inhibition in packed-bed re-circulated Immobilized Enzyme reactors is presented, where the use of nonlinear regression techniques for multi-parameter estimation are not required. In order to demonstrate the new technique introduced in this work, enzymatic conversion of lactose in a recycling packed-bed reactor is envisaged where β-galactosidase (lactase, EC 3.2.1.23) Enzyme is Immobilized on a weak base ion exchanger resin (Duolite A 568). For the experimental conditions used in this research, the total competitive inhibition by product (galactose) model is sufficient to represent the lactose hydrolysis kinetics in a packed-bed reactor.
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a new method for determination of apparent kinetics parameters in recirculating packed bed Immobilized Enzyme reactors
Chemical Engineering Science, 2001Co-Authors: Ahmet R Ozdural, Zafer Demircan, Deniz Tanyolac, Ismail Hakki Boyaci, Mehmet MutluAbstract:Abstract In this study, a simple and effective technique for characterizing Michaelis–Menten apparent kinetic parameters in packed-bed Immobilized Enzyme reactors is presented. The apparent kinetic parameters of Immobilized glucose oxidase on weak base ion exchanger resin (Duolite A 568) were determined for different substrate flow rates in a recirculation system and compared with those for soluble glucose oxidase. It was observed that, for the experimental conditions, the Immobilized Enzyme K ′ m values in a packed-bed reactor were less than the soluble Enzyme K m value and were flow dependent. The value of K ′ m decreased with increasing flow rate.
Hai Wang - One of the best experts on this subject based on the ideXlab platform.
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papain zn3 po4 2 hybrid nanoflower preparation characterization and its enhanced catalytic activity as an Immobilized Enzyme
RSC Advances, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Lili Fan, Qiuyu ZhangAbstract:Flower-like papain/Zn3(PO4)2 hybrid materials are synthesized via a facile, rapid and low-cost method in this study. The growth process of the nanoflowers has been studied in detail and a four-step formation mechanism, including coordination, precipitation, self-assembly and size growth, has been clarified. The concentration of papain mainly affects the morphology of the products by regulating the assembly and crystal growth. The Enzyme activity of papain/Zn3(PO4)2 hybrid nanoflowers, a novel Immobilized Enzyme, was calculated by monitoring the hydrolysis reaction of casein. The results show that the catalytic properties of papain Immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The as-prepared hybrid nanoflowers exhibited excellent reusability, high thermo stability and long storage life. The results indicate that the well-designed materials have great potential in industrial applications.
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preparation of lipase zn3 po4 2 hybrid nanoflower and its catalytic performance as an Immobilized Enzyme
Chemical Engineering Journal, 2016Co-Authors: Baoliang Zhang, Hepeng Zhang, Hai Wang, Lei Tian, Nisar Ali, Zafar Ali, Qiuyu ZhangAbstract:Abstract A facile and rapid method is reported in this paper to prepare a novel Immobilized Enzyme named lipase/Zn3(PO4)2 hybrid nanoflower. The growth mechanism of the nanoflower has been studied in detail and can be described as the following four steps: crystallization and coordination, in-situ precipitation, self-assembly, size growth. Addition amount of lipase, reaction temperature and stirring form affect the morphology and lipase content of the hybrid nanoflower. Besides, the catalytic performance of lipase/Zn3(PO4)2 hybrid nanoflower was investigated and the optimal catalytic conditions have been found. The maximum Enzyme activity was 855 ± 13 U/g. In comparison with the free lipase, the Enzyme activity increment of hybrid nanoflower is 147%. Meanwhile, the unique nanostructure makes lipase/Zn3(PO4)2 hybrid nanoflower an excellent operational stabilizer. The results indicate that the well-designed materials should be useful in industrial Enzyme catalysis.
