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小麦秸秆发酵产生的真菌Pleurotus ostreatus IBL-02锰过氧化物酶的溶胶-凝胶固定化及其催化污水脱色(英文) 被引量:4
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作者 Muhammad Asgher Bazgha Aslam +1 位作者 Hafiz Muhammad Nasir Iqbal 《催化学报》 SCIE EI CAS CSCD 北大核心 2013年第9期1756-1761,共6页
Solid state bio-processing of wheat straw was carried out through an indigenous fungal strain Pleurotus ostreatus IBL-02 under pre-optimized fermentation conditions. The maximum activity, 692±12 U/mL, of the indu... Solid state bio-processing of wheat straw was carried out through an indigenous fungal strain Pleurotus ostreatus IBL-02 under pre-optimized fermentation conditions. The maximum activity, 692±12 U/mL, of the industrially important manganese peroxidase (MnP) enzyme was recorded after five days of still culture incubation. The crude MnP was 2.1-fold purified with a specific activity of 860 U/mg after purification on a Sephadex-G-100 gel column. On native and SDS-PAGE electrophoresis gels, the purified MnP fraction was a single homogenous band of 45 kDa. An active fraction of MnP was immobilized using hydrophobic sol-gel entrapment comprising tetramethoxysilane (T) and propyltrimethoxysilane (P) at different T:P molar ratios. Characterization revealed that after 24 h incubation at varying pH and temperatures, the MnP fraction immobilized at a T:P ratio of 1:2 in the sol-gel retained 82% and 75% of its original activity at pH4 and 70 ℃, respectively. The optimally active fraction at a 1:2 T:P ratio was tested against MnSO4 as a substrate to determine the kinetic catalytic constants KM and Vmax . To explore the industrial applicability of P. ostreatus IBL-02 MnP, both the free and immobilized MnP were used for the decolorization of four different textile industrial effluents. A maximum of 100% decolorization was achieved for the different textile effluents within the shortest time period. A lower KM , higher Vmax , hyper-activation, and enhanced acidic and thermal resistance up to 70 ℃ were the novel catalytic features of the sol-gel immobilized MnP, suggesting that it may be a potential candidate for biotechnological applications particularly for textile bioremediation purposes. 展开更多
关键词 PLEUROTUS ostreatus IBL-02 bio-catalysis Manganese PEROXIDASE Immobilization Sol-gel Textile effluent DECOLORIZATION
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Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis 被引量:2
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作者 Shanshan Pei Xiaobo Ruan +5 位作者 Jia Liu Wei Song Xiulai Chen Qiuling Luo Liming Liu Jing Wu 《Chinese Journal of Chemical Engineering》 SCIE EI CAS CSCD 2020年第8期2190-2199,共10页
L-Amino acid deaminase(LAAD) is a key enzyme in the deamination of L-valine(L-val) to produce α-ketoisovalerate(KIV). However, the product inhibition of LAAD is a major hindrance to industrial KIV production.In the p... L-Amino acid deaminase(LAAD) is a key enzyme in the deamination of L-valine(L-val) to produce α-ketoisovalerate(KIV). However, the product inhibition of LAAD is a major hindrance to industrial KIV production.In the present study, a combination strategy of modification of flexible loop regions around the product binding site and the avoidance of dramatic change of main-chain dynamics was reported to reduce the product inhibition.The four mutant PM-LAAD^(M4)(PM-LAAD^(S98A/T105A/S106A/L341A)) achieved a 6.2-fold higher catalytic efficiency and an almost 6.7-fold reduction in product inhibition than the wild-type enzyme. Docking experiments suggested that weakened interactions between the product and enzyme, and the flexibility of the "lid" structure relieved LAAD product inhibition. Finally, the whole-cell biocatalyst PM-LAAD^(M4) has been applied to KIV production,the titer and conversion rate of KIV from L-val were 98.5 g·L^-1 and 99.2% at a 3-L scale, respectively. These results demonstrate that the newly engineered catalyst can significantly reduce the product inhibition, that making KIV a prospective product by bioconversion method, and also provide the understanding of the mechanism of the relieved product inhibition of PM-LAAD. 展开更多
关键词 Product inhibition L-Amino acid deaminases α-Ketoisovalerate bio-catalysis Protein engineering
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Enhanced bio-catalytic and tolerance properties of an indigenous cellulase through xerogel immobilization 被引量:1
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作者 Hafiz Muhammad Nasir Iqbal Shagufta Kamal +1 位作者 Ishtiaq Ahmed Muhammad Tahir Naveed 《Advances in Bioscience and Biotechnology》 2012年第4期308-313,共6页
Today, demand exists for cost-effective production of industrially important enzymes from entire scientific sectors. By keeping in mind the extensive industrial applications of cellulase, this study was performed to i... Today, demand exists for cost-effective production of industrially important enzymes from entire scientific sectors. By keeping in mind the extensive industrial applications of cellulase, this study was performed to immobilize the indigenous enzyme produced from Trichoderma viride under pre-optimized SSF of an agricultural waste material, wheat straw. To enhance the bio-catalytic and tolerance properties of the present enzyme gel matrix immobilization engineering was applied. Previously, 2.33~fold purified novel cellulase was immobilized in to a xerogel matrix of TMOS and PTMS. FTIR spectroscopy confirmed the successful immobilization of cellulase. The free and immobilized cellulase was characterized and stability profile showed that after 24 h incubation, immobilization enhanced the thermo-stability up to 75% against 80℃ as compare to the free enzyme. Xerogel matrix immobilization enhanced the catalytic efficiency of entrapped enzyme than that of the free cellulase. Among activators/inhibitors SDS, EDTA, and Hg2+ showed inhibitory effect while, gel matrix immobilization enhanced 80% tolerance capacity of the cellulase against inactivating agents. 展开更多
关键词 bio-catalysis CELLULASE T. viride IMMOBILIZATION Characterization
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PREPARATION OF UREA NITROGEN ADSORBENT OF COMPLEX TYPE AND ADSORPTION CAPACITY OF UREA NITROGEN ONTO THE ADSORBENT
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作者 梁足培 冯亚青 +1 位作者 梁智妍 孟舒献 《Transactions of Tianjin University》 EI CAS 2006年第1期37-41,共5页
The urea nitrogen adsorbent of complex type, which consists of chitosan coated dialdehyde cellulose (CDAC) and immobilized urease in gelatin membrane (IE), was prepared. The cellulose, the dialdehyde cellulose (... The urea nitrogen adsorbent of complex type, which consists of chitosan coated dialdehyde cellulose (CDAC) and immobilized urease in gelatin membrane (IE), was prepared. The cellulose, the dialdehyde cellulose (DAC) and the CDAC were characterized by scanning electronic microscope. The results indicate that the cellulose C2-C3 bond was broken under the oxidation of periodate and it was oxidated to DAC. The DAC was coated with chitosan and the CDAC was obtained. The adsorption of urea nitrogen onto the adsorbent in Na2HPO4-NaH2PO4 buffer solution was studied in batch system. The effects of the experiment parameters, including degree of oxidation of CDAC, initial urea nitrogen concentration, pH and temperature, on the adsorption capacity of urea nitrogen onto the adsorbent at CDAC/IE weight ratio 10:1 were investigated. The results indicate that these parameters affected significantly the adsorption capacity. The adsorption capacity of urea nitrogen onto the adsorbent was 36.7 mg/g at the degree of oxidation of CDAC 88%, initial urea nitrogen concentration 600 mg/L, pH 7.4 and temperature 37℃. 展开更多
关键词 adsorption urea nitrogen complex type adsorbent chitosan coated dialdehyde cellulose immobilized urease bio-catalysis
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