Preparative Biochemistry & Biotechnology最新文献_第10页

Kinetic and thermodynamic investigation of Rhodanese synthesized by enhanced Klebsiella oxytoca JCM 1665 strain: a comparative between the free and immobilized enzyme entrapped in alginate beads. 增强型氧合克雷伯氏菌 JCM 1665 菌株合成罗丹酶的动力学和热力学研究：游离酶与海藻酸珠子固定酶的比较。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-05-02 DOI: 10.1080/10826068.2024.2347407

Babamotemi Oluwasola Itakorode, Dorcas Ibukunoluwa Itakorode, Nkem Torimiro, Raphael Emuebie Okonji

{"title":"Kinetic and thermodynamic investigation of Rhodanese synthesized by enhanced Klebsiella oxytoca JCM 1665 strain: a comparative between the free and immobilized enzyme entrapped in alginate beads.","authors":"Babamotemi Oluwasola Itakorode, Dorcas Ibukunoluwa Itakorode, Nkem Torimiro, Raphael Emuebie Okonji","doi":"10.1080/10826068.2024.2347407","DOIUrl":"10.1080/10826068.2024.2347407","url":null,"abstract":"Klebsiella oxytoca JCM 1665 was subjected to extracellular rhodanese production using a submerged fermentation technique. The organism was further engineered for higher cyanide tolerance and rhodanese yield using ethylmethanesulfonate as a mutagen. Mutagenesis resulted in an improved mutant with high cyanide tolerance (100 mM) and rhodanese yield (26.7 ± 0.67 U/mL). This yield was 4.34-fold higher than the wild strain (6.15 ± 0.65 U/mL). At temperatures ranging from 30 to 80 °C, the first-order thermal denaturation constant (Kd) for free enzyme increases from 0.00818 to 0.0333 min-1 while the immobilized enzyme increases from 0.003 to 0.0204 min-1. The equivalent half-life reduces from 99 to 21 minutes and 231 to 35 minutes, respectively. Residual activity tests were used to assess the thermodynamic parameters for both enzyme preparations. For the free enzyme, the parameters obtained were enthalpy (29.40 to 29.06 kJ.mol-1), entropy (-194.24 to -197.50 J.mol-1K-1) and Gibbs free energy (90.20 to 98.80 kJ.mol-1). In addition, for immobilized rhodanese, we obtained enthalpy (40.40 to 40.07 kJ.mol-1), entropy (-164.21 to - 165.20 J.mol-1K-1) and Gibbs free energy (91.80 to 98.40 kJ.mol-1. Regarding its operational stability, the enzyme was able to maintain 63% of its activity after being used for five cycles. Immobilized K. oxytoca rhodanese showed a marked resistance to heat inactivation compared to free enzyme forms; making it of utmost significance in many biotechnological applications.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1275-1284"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140864722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Biochemical characterization, stability, and kinetics of three substrates of the recombinant TMPRSS2 serine protease domain. 重组 TMPRSS2 丝氨酸蛋白酶结构域三种底物的生化特性、稳定性和动力学。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-05-10 DOI: 10.1080/10826068.2024.2349132

Flávio Antônio de Oliveira-Simões, Isabela Victorino da Silva Amatto, Camila Langer Marciano, Nathalia Gonsales da Rosa-Garzon, Débora Noma Okamoto, Maria Aparecida Juliano, Luiz Juliano, Hamilton Cabral

{"title":"Biochemical characterization, stability, and kinetics of three substrates of the recombinant TMPRSS2 serine protease domain.","authors":"Flávio Antônio de Oliveira-Simões, Isabela Victorino da Silva Amatto, Camila Langer Marciano, Nathalia Gonsales da Rosa-Garzon, Débora Noma Okamoto, Maria Aparecida Juliano, Luiz Juliano, Hamilton Cabral","doi":"10.1080/10826068.2024.2349132","DOIUrl":"10.1080/10826068.2024.2349132","url":null,"abstract":"Transmembrane serine protease 2 (TMPRSS2) is a membrane-bound protease belonging to the type II transmembrane serine protease (TTSP) family. It is a multidomain protein, including a serine protease domain responsible for its self-activation. The protein has been implicated as an oncogenic transcription factor and for its ability to cleave (prime) the SARS-CoV-2 spike protein. In order to characterize the TMPRSS2 biochemical properties, we expressed the serine protease domain (rTMPRSS2_SP) in Komagataella phaffii using the pPICZαA vector and purified it using immobilized metal affinity (Ni Sepharose™ excel) and size exclusion (Superdex 75) chromatography. We explored operational fluorescence resonance energy transfer FRET peptides as substrates. We chose the peptide Abz-QARK-(Dnp)-NH2 (Abz = ortho-aminobenzoic acid, the fluorescence donor, and Dnp = 2,4-dinitrophenyl, the quencher group) as a substrate to find the optimal conditions for maximum enzymatic activity. We found that metallic ions such as Ca2+ and Na+ increased enzymatic activity, but ionic surfactants and reducing agents decreased catalytic capacity. Finally, we determined the rTMPRSS2_SP stability for long-term storage. Altogether, our results represent the first comprehensive characterization of TMPRSS2's biochemical properties, providing valuable insights into its serine protease domain.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1285-1293"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140898876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A comprehensive study of glucose and oxygen gradients in a scaled-down model of recombinant HuGM-CSF production in thermoinduced Escherichia coli fed-batch cultures. 在热诱导大肠杆菌分批进行喂养培养的重组 HuGM-CSF 生产缩减模型中对葡萄糖和氧气梯度的综合研究。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-05-03 DOI: 10.1080/10826068.2024.2347403

Greta I Reynoso-Cereceda, Norma A Valdez-Cruz, Nestor O Pérez, Mauricio A Trujillo-Roldán

{"title":"A comprehensive study of glucose and oxygen gradients in a scaled-down model of recombinant HuGM-CSF production in thermoinduced Escherichia coli fed-batch cultures.","authors":"Greta I Reynoso-Cereceda, Norma A Valdez-Cruz, Nestor O Pérez, Mauricio A Trujillo-Roldán","doi":"10.1080/10826068.2024.2347403","DOIUrl":"10.1080/10826068.2024.2347403","url":null,"abstract":"The effect of gradients of elevated glucose and low dissolved oxygen in the addition zone of fed-batch E. coli thermoinduced recombinant high cell density cultures can be evaluated through two-compartment scale-down models. Here, glucose was fed in the inlet of a plug flow bioreactor (PFB) connected to a stirred tank bioreactor (STB). E. coli cells diminished growth from 48.2 ± 2.2 g/L in the stage of RP production if compared to control (STB) with STB-PFB experiments, when residence time inside the PFB was 25 s (34.1 ± 3.5 g/L) and 40 s (25.6 ± 5.1 g/L), respectively. The recombinant granulocyte-macrophage colony-stimulating factor (rHuGM-CSF) production decreased from 34 ± 7% of RP in inclusion bodies (IB) in control cultures to 21 ± 8%, and 7 ± 4% during the thermoinduction production phase when increasing residence time inside the PFB to 25 s and 40 s, respectively. This, along with the accumulation of acetic and formic acid (up to 4 g/L), indicates metabolic redirection of central carbon routes through metabolic flow and mixed acid fermentation. Special care must be taken when producing a recombinant protein in heat-induced E. coli, because the yield and productivity of the protein decreases as the size of the bioreactors increases, especially if they are carried at high cell density.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1263-1274"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140862958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Isolation, characterization and optimization of oleaginous Providencia vermicola as a feedstock for biodiesel production using Response Surface Methodology. 利用响应面方法对作为生物柴油生产原料的含油蛭藻进行分离、表征和优化。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-05-10 DOI: 10.1080/10826068.2024.2344516

Temitope Abiola, Olumide D Olukanni

{"title":"Isolation, characterization and optimization of oleaginous Providencia vermicola as a feedstock for biodiesel production using Response Surface Methodology.","authors":"Temitope Abiola, Olumide D Olukanni","doi":"10.1080/10826068.2024.2344516","DOIUrl":"10.1080/10826068.2024.2344516","url":null,"abstract":"Oleaginous organisms accrue more than twenty percent of their biomass as lipids and hence are promising feedstocks for biodiesel production. In this study, lipid accumulating bacteria were isolated from diesel-contaminated soils and screened with Sudan black B stain. The most oleaginous was done using 16s rRNA gene sequencing. Lipid production was initially optimized based on media, nitrogen source, pH and temperature. Response surface methodology (RSM) was then employed for the enhancement of lipid weight and content. Obtained lipid was converted to biodiesel using direct transesterification, and both lipid and biodiesel were characterized using FTIR. A total of thirteen bacteria were isolated and the most prominent lipid producer was identified as Providencia vermicola with lab number BA6. Preliminary optimization studies revealed optimum lipid production when nutrient broth and acetic acid served as carbon source; KNO3 as nitrogen source, pH 7.0 and 30 °C. Optimization using RSM resulted in a 5.1% and 74.1% increase in the biomass and lipid content of BA6 respectively. FTIR analyses confirmed the presence of functional groups characteristic of lipids and biodiesel. P. vermicola is a novel oleaginous organism that represents a promising feedstock for biodiesel production.HIGHLIGHTSThe bacterium designated as BA6 identified as Providencia vermicola has the highest lipid contents of the oleaginous bacteria isolated.It accumulates lipids up to 47.73 % of its biomassThe percentage lipids accumulation increased to about 74 % when RSM was used.Providencia vermicola is being reported as an oleaginous organism for the first time.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1226-1242"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140898877","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Resin screening and process optimization for erythritol mother liquor chromatographic separation. 用于赤藓糖醇母液色谱分离的树脂筛选和工艺优化。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-05-14 DOI: 10.1080/10826068.2024.2349936

Haiyang Li, Xiangying Zhao, Liping Liu, Mingjing Yao, Yanlei Han, Ruiguo Li, Jianjun Liu, Jiaxiang Zhang

{"title":"Resin screening and process optimization for erythritol mother liquor chromatographic separation.","authors":"Haiyang Li, Xiangying Zhao, Liping Liu, Mingjing Yao, Yanlei Han, Ruiguo Li, Jianjun Liu, Jiaxiang Zhang","doi":"10.1080/10826068.2024.2349936","DOIUrl":"10.1080/10826068.2024.2349936","url":null,"abstract":"In order to improve the utilization value of the erythritol mother liquor, the separation and purification of the erythritol mother liquor was selected in this study. The selected chromatographic separation programme for erythritol crystallizing mother liquor is as follows: Firstly, erythritol is resolved from mannitol and arabitol with DTF-01Ca (Suqing Group) resin and then mannitol is resolved from arabitol with 99Ca/320 (Dowex) resin. At the same time, the chromatographic conditions of the DTF-01Ca (Suqing Group) and 99Ca/320 (Dowex) resins were optimized, resulting in an optimal separation temperature and mobile phase flow rate of 70 °C, 10 ml/min. On this basis, a single-column chromatographic model was used to calculate the TD model parameter (<math><mrow><mi>N</mi></mrow></math>) and the mass transfer coefficient (<math><msub><mrow><mi>k</mi></mrow><mrow><mi>m</mi><mi> </mi></mrow></msub></math>) of the separation of erythritol mother liquor by DTF-01Ca (Suqing Group) and 99Ca/320 (Dowex) resins. The adsorption isotherms, TD model parameter (<math><mrow><mi>N</mi></mrow></math>) and the mass transfer coefficient (<math><msub><mrow><mi>k</mi></mrow><mrow><mi>m</mi><mi> </mi></mrow></msub></math>) provides data references for the design and operation of the simulated moving beds (SMB) separation system for the industrial-scale separation of erythritol crystallizing mother liquor.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1294-1305"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140922863","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Utilization of low-grade walnut kernels for oil extraction using eco-friendly methods: a comparative analysis of oil composition, antioxidant and antimicrobial activity. 利用生态友好型方法提取低级核桃仁油：油成分、抗氧化剂和抗菌活性的比较分析。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-11-01 Epub Date: 2024-07-16 DOI: 10.1080/10826068.2024.2345244

Iqra Mohiuddin Bhat, Shoib Mohmad Wani, Sajad Ahmad Mir, Farooq A Masoodi, Saiqa Bhat

{"title":"Utilization of low-grade walnut kernels for oil extraction using eco-friendly methods: a comparative analysis of oil composition, antioxidant and antimicrobial activity.","authors":"Iqra Mohiuddin Bhat, Shoib Mohmad Wani, Sajad Ahmad Mir, Farooq A Masoodi, Saiqa Bhat","doi":"10.1080/10826068.2024.2345244","DOIUrl":"10.1080/10826068.2024.2345244","url":null,"abstract":"Walnut oil was extracted using three different eco-friendly extraction methods, solvent extraction (using ethyl acetate [EA] and ethanol [ET]), aqueous enzymatic extraction (AEE), and ultrasound-assisted enzymatic extraction (UAEE), and their lipid yield, lipid composition, physicochemical analysis, mineral composition, total phenols, antioxidant capacity, and antimicrobial activity were analyzed and compared. The AEE technique offered a greater yield (50.6%) than the other extraction methods and gave comparatively higher linoleic acid (66.12%) content. Palmitic, oleic, linoleic, linolenic, and stearic acids were the principal components that GC/MS detected in all the oil samples. UAEE produced the most polyphenols (0.49 mgGAE/g), followed by AEE (0.46 mgGAE/g), EA (0.45 mgGAE/g), and ET (0.35 mgGAE/g). The DPPH assay results were in the order of UAEE (191 μmolTE/kg) > AEE (186 μmolTE/kg) > EA (153 μmolTE/kg) > ET (130 μmolTE/kg). The FRAP assay findings showed a similar pattern: UAEE (112 molTE/kg) > AEE (102 molTE/kg) > EA (96 molTE/kg) > ET (82 molTE/kg). Results suggested that for a higher extraction yield, AEE is the better technique and UAEE is the recommended method for enhancing walnut oil antioxidant capacity. Additionally, it was found that polyphenols considerably increased the antioxidant capacity of walnut oil and are thought to be health-promoting. The results demonstrated the antibacterial effectiveness of the extracted oil against Bacillus subtilis, Bacillus licheniformis, and Staphylococcus aureus. This study provides information about low-cost and ecofriendly technologies of walnut oil extraction for food, cosmetic, and medical uses.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1243-1252"},"PeriodicalIF":2.0,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141620750","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Application of membrane separation technology in the purification of pharmaceutical components. 膜分离技术在药物成分纯化中的应用。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-10-01 Epub Date: 2024-03-25 DOI: 10.1080/10826068.2024.2328673

Yun Bi, Jingyi Dong, Yujia Zhou, Manyue Zhang, Xingying Chen, Yuyan Zhang

引用次数: 0

Microwave-enhanced hydrolysis of cellulose by acidic ionic liquids. 微波增强酸性离子液体对纤维素的水解作用。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-10-01 Epub Date: 2024-03-23 DOI: 10.1080/10826068.2024.2333467

Meng-Meng Liu, Liang-Yan Zhang, Zhen Liu

引用次数: 0

Statistical versus neural network-embedded swarm intelligence optimization of a metallo-neutral-protease production: activity kinetics and food industry applications. 金属中性蛋白酶生产的统计与神经网络嵌入式群集智能优化：活性动力学与食品工业应用。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-10-01 Epub Date: 2024-03-16 DOI: 10.1080/10826068.2024.2328681

Maurice George Ekpenyong, Sylvester Peter Antai

{"title":"Statistical versus neural network-embedded swarm intelligence optimization of a metallo-neutral-protease production: activity kinetics and food industry applications.","authors":"Maurice George Ekpenyong, Sylvester Peter Antai","doi":"10.1080/10826068.2024.2328681","DOIUrl":"10.1080/10826068.2024.2328681","url":null,"abstract":"An integrated approach involving response surface methodology (RSM) and artificial neural network-ant-colony hybrid optimization (ANN-ACO) was adopted to develop a bioprocess medium to increase the yield of Bacillus cereus neutral protease under submerged fermentation conditions. The ANN-ACO model was comparatively superior (predicted r2 = 98.5%, mean squared error [MSE] = 0.0353) to RSM model (predicted r2 = 86.4%, MSE = 23.85) in predictive capability arising from its low performance error. The hybrid model recommended a medium containing (gL-1) molasses 45.00, urea 9.81, casein 25.45, Ca2+ 1.23, Zn2+ 0.021, Mn2+ 0.020, and 4.45% (vv-1) inoculum, for a 6.75-fold increase in protease activity from a baseline of 76.63 UmL-1. Yield was further increased in a 5-L bioreactor to a final volumetric productivity of 3.472 mg(Lh)-1. The 10.0-fold purified 46.6-kDa-enzyme had maximum activity at pH 6.5, 45-55 °C, with Km of 6.92 mM, Vmax of 769.23 µmolmL-1 min-1, kcat of 28.49 s-1, and kcat/Km of 4.117 × 103 M-1 s-1, at 45 °C, pH 6.5. The enzyme was stabilized by Ca2+, activated by Zn2+ but inhibited by EDTA suggesting that it was a metallo-protease. The biomolecule significantly clarified orange and pineapple juices indicating its food industry application.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1132-1146"},"PeriodicalIF":2.0,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140140627","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Valorization of sugarcane bagasse for high-yield production of laccase through Aspergillus terreus for effective azo dye decolourization. 利用甘蔗渣的价值，通过土曲霉高产生产漆酶，有效去除偶氮染料。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-10-01 Epub Date: 2024-04-01 DOI: 10.1080/10826068.2024.2332881

T Chandukishore, Tuhin Subhra Biswas, Ashish A Prabhu

{"title":"Valorization of sugarcane bagasse for high-yield production of laccase through Aspergillus terreus for effective azo dye decolourization.","authors":"T Chandukishore, Tuhin Subhra Biswas, Ashish A Prabhu","doi":"10.1080/10826068.2024.2332881","DOIUrl":"10.1080/10826068.2024.2332881","url":null,"abstract":"Synthetic dyes such as azo dyes are significant pollutants in the wastewater released from various textile industries. The low biodegradability and production from synthetic sources with high shelf life make azo dyes a challenging material for degradation. This study used chemically mutated Aspergillus terrus in the laccase production under solid-state fermentation using sugarcane bagasse. Initially, the wild-type strain produced a laccase activity of 4.12 U/mL. Later, the alkaline pretreatment of sugarcane bagasse showed a significant increase in laccase activity by 38.9%. Further, random mutagenesis treatment with 100 mM EMS generated a hyper laccase-producing strain with a 2.3-fold increment in laccase activity compared to the wild-type strain. The enzyme displayed optimal activity at pH 6.5 and 35 °C. The metal ions such as Fe3+ (29.4 U/mL), Fe2+ (20.8 U/mL) and Cu2+ (18.05 U/mL) showed positive effects on laccase activity. The crude laccase was used to bioremediate Congo red, a prominent azo dye used in textile and pharmaceutical industries. The preliminary studies with a crude enzyme displayed 68.86% dye decolourization after 24 h of incubation. Additionally, with Taguchi orthogonal array optimization experiments, the maximal dye decolorization of 78.24% was achieved by maintaining crude enzyme concentration (20 U), dye concentration (25 mg/L) and pH 4.5.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1170-1181"},"PeriodicalIF":2.0,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140336649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0