Preparative Biochemistry and Biotechnology最新文献

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Bioprocess optimization for production of thermoalkali-stable protease from Bacillus subtilis K-1 under solid-state fermentation 枯草芽孢杆菌K-1固态发酵产热碱稳定蛋白酶的生物工艺优化
Preparative Biochemistry and Biotechnology Pub Date : 2016-01-13 DOI: 10.1080/10826068.2015.1135455
Satbir Singh, B. K. Bajaj
{"title":"Bioprocess optimization for production of thermoalkali-stable protease from Bacillus subtilis K-1 under solid-state fermentation","authors":"Satbir Singh, B. K. Bajaj","doi":"10.1080/10826068.2015.1135455","DOIUrl":"https://doi.org/10.1080/10826068.2015.1135455","url":null,"abstract":"ABSTRACT Cost-effective production of proteases, which are robust enough to function under harsh process conditions, is always sought after due to their wide industrial application spectra. Solid-state production of enzymes using agro-industrial wastes as substrates is an environment-friendly approach, and it has several advantages such as high productivity, cost-effectiveness, being less labor-intensive, and less effluent production, among others. In the current study, different agro-wastes were employed for thermoalkali-stable protease production from Bacillus subtilis K-1 under solid-state fermentation. Agricultural residues such as cotton seed cake supported maximum protease production (728 U ml−1), which was followed by gram husk (714 U ml−1), mustard cake (680 U ml−1), and soybean meal (653 U ml−1). Plackett–Burman design of experiment showed that peptone, moisture content, temperature, phosphates, and inoculum size were the significant variables that influenced the protease production. Furthermore, statistical optimization of three variables, namely peptone, moisture content, and incubation temperature, by response surface methodology resulted in 40% enhanced protease production as compared to that under unoptimized conditions (from initial 728 to 1020 U ml−1). Thus, solid-state fermentation coupled with design of experiment tools represents a cost-effective strategy for production of industrial enzymes.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83587077","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 32
Cloning, expression, and characterization of catechol 1,2-dioxygenase from a phenol-degrading Candida tropicalis JH8 strain 苯酚降解热带假丝酵母JH8菌株儿茶酚1,2-双加氧酶的克隆、表达和特性研究
Preparative Biochemistry and Biotechnology Pub Date : 2016-01-13 DOI: 10.1080/10826068.2015.1135449
Yan Long, Sheng Yang, Zhixiong Xie, Li-Li Cheng
{"title":"Cloning, expression, and characterization of catechol 1,2-dioxygenase from a phenol-degrading Candida tropicalis JH8 strain","authors":"Yan Long, Sheng Yang, Zhixiong Xie, Li-Li Cheng","doi":"10.1080/10826068.2015.1135449","DOIUrl":"https://doi.org/10.1080/10826068.2015.1135449","url":null,"abstract":"ABSTRACT The sequence cato encoding catechol 1,2-dioxygenase from Candida tropicalis JH8 was cloned, sequenced, and expressed in Escherichia coli. The sequence cato contained an ORF of 858 bp encoding a polypeptide of 285 amino acid residues. The recombinant catechol 1,2-dioxygenase exists as a homodimer structure with a subunit molecular mass of 32 KD. Recombinant catechol 1,2-dioxygenase was unstable below pH 5.0 and stable from pH 7.0 to 9.0; its optimum pH was at 7.5. The optimum temperature for the enzyme was 30°C, and it possessed a thermophilic activity within a broad temperature range. Under the optimal conditions with catechol as substrate, the Km and Vmax of recombinant catechol 1,2-dioxygenase were 9.2 µM and 0.987 µM/min, respectively. This is the first article presenting cloning and expressing in E. coli of catechol 1,2-dioxygenase from C. tropicalis and characterization of the recombinant catechol 1,2-dioxygenase.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85711829","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 10
Development of a low-serum medium for the production of monoclonal antibody against congenital adrenal hyperplasia by hybridoma culture 用杂交瘤培养生产抗先天性肾上腺增生单克隆抗体的低血清培养基的研制
Preparative Biochemistry and Biotechnology Pub Date : 2016-01-13 DOI: 10.1080/10826068.2015.1135450
G. K. Chua
{"title":"Development of a low-serum medium for the production of monoclonal antibody against congenital adrenal hyperplasia by hybridoma culture","authors":"G. K. Chua","doi":"10.1080/10826068.2015.1135450","DOIUrl":"https://doi.org/10.1080/10826068.2015.1135450","url":null,"abstract":"ABSTRACT Statistically designed experiments were used in developing a low-serum medium for the production of a diagnostic monoclonal antibody against congenital adrenal hyperplasia using hybridoma 192. A two-level half-fractional factorial design was used for screening six components (Minimum Essential Medium Eagle amino acids, 2-mercaptoethanol, ethanolamine, ferric citrate, zinc sulfate, and sodium selenite). The experimental design was then augmented to central composite design. The basal Dulbecco’s modified Eagle’s medium (DMEM; containing 4 mM L-glutamine, 1% antibiotic–antimycotic agent) supplemented with 0.4% by volume fetal bovine serum (FBS), 311.8 mM ferric citrate, 17.3 nM sodium selenite, and 4.5 mM zinc sulfate (LSD) was found to support the growth of the hybridoma. Specific cell growth rate in the LSD (0.033 ± 0.001/h) was slightly lower than in the control medium (i.e., basal DMEM supplemented with 2% FBS; 0.0045 ± 0.003/h). Nevertheless, the specific MAb production rate for LSD was higher (0.057 ± 0.015 pg/cell · h versus 0.004 ± 0.002 pg/cell · h in LSD and control, respectively). The antibody produced in the LSD showed high specificity and no cross-reactivity with the other structural resemblance’s steroid hormones, revealing no structural changes owing to the new medium formulation developed. The new medium formulation effectively reduced the medium cost by up to 64.6%.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82165582","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1
Impact of microbial growth inhibition and proteolytic activity on the stability of a new formulation containing a phytate-degrading enzyme obtained from mushroom 微生物生长抑制和蛋白水解活性对蘑菇植酸降解酶新配方稳定性的影响
Preparative Biochemistry and Biotechnology Pub Date : 2016-01-13 DOI: 10.1080/10826068.2015.1135456
M. R. Spier, F. B. Siepmann, Larissa Staack, P. Z. Souza, Vikas Kumar, A. Medeiros, C. R. Soccol
{"title":"Impact of microbial growth inhibition and proteolytic activity on the stability of a new formulation containing a phytate-degrading enzyme obtained from mushroom","authors":"M. R. Spier, F. B. Siepmann, Larissa Staack, P. Z. Souza, Vikas Kumar, A. Medeiros, C. R. Soccol","doi":"10.1080/10826068.2015.1135456","DOIUrl":"https://doi.org/10.1080/10826068.2015.1135456","url":null,"abstract":"ABSTRACT The development of stable enzymes is a key issue in both the food and feed industries. Consequently, the aim of the current study is to evaluate the impact of various additives (sodium chloride, sodium citrate, mannitol, methylparaben, polyethylene glycol 3350, ethylenediaminetetraacetic acid disodium salt, and a serine protease inhibitor) on the stability of a mushroom phytase produced by solid-state cultivation and recovery. Also observed was the effect of the additives on microbial growth inhibition by monitoring both the change in optical density over 30 days of storage and proteolytic activity. Initially, eight experimental formulations were prepared along with a control. After screening, a 32 factorial design was applied to define suitable concentrations of the selected additives. Among the eight formulations tested, the formulation containing NaCl, PEG 3350, and methylparaben retained all of the initial phytase activity after 50 days of storage, with no detected interference from protease activity. Sodium citrate, a metal chelation agent, presented the unusual effect of reducing protease activity in the formulations. Although all formulations presented better phytase stability when compared to the control, NaCl and PEG were both able to prolong the stability of the enzyme activity and also to inhibit microbial growth during storage, making them favorable for application as food and feed additives.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72784356","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 3
Development of a semidefined growth medium for Pedobacter cryoconitis BG5 using statistical experimental design 采用统计实验设计开发一种半确定的冷冻结肠炎杆菌BG5生长培养基
Preparative Biochemistry and Biotechnology Pub Date : 2016-01-13 DOI: 10.1080/10826068.2015.1135447
M. Ong, Clarence M. Ongkudon, C. Wong
{"title":"Development of a semidefined growth medium for Pedobacter cryoconitis BG5 using statistical experimental design","authors":"M. Ong, Clarence M. Ongkudon, C. Wong","doi":"10.1080/10826068.2015.1135447","DOIUrl":"https://doi.org/10.1080/10826068.2015.1135447","url":null,"abstract":"ABSTRACT Pedobacter cryoconitis BG5 are psychrophiles isolated from the cold environment and capable of proliferating and growing well at low temperature regime. Their cellular products have found a broad spectrum of applications, including in food, medicine, and bioremediation. Therefore, it is imperative to develop a high-cell density cultivation strategy coupled with optimized growth medium for P. cryoconitis BG5. To date, there has been no published report on the design and optimization of growth medium for P. cryoconitis, hence the objective of this research project. A preliminary screening of four commercially available media, namely tryptic soy broth, R2A, Luria Bertani broth, and nutrient broth, was conducted to formulate the basal medium. Based on the preliminary screening, tryptone, glucose, NaCl, and K2HPO4 along with three additional nutrients (yeast extract, MgSO4, and NH4Cl) were identified to form the basal medium which was further analyzed by Plackett–Burman experimental design. Central composite experimental design using response surface methodology was adopted to optimize tryptone, yeast extract, and NH4Cl concentrations in the formulated growth medium. Statistical data analysis showed a high regression factor of 0.84 with a predicted optimum optical (600 nm) cell density of 7.5 using 23.7 g/L of tryptone, 8.8 g/L of yeast extract, and 0.7 g/L of NH4Cl. The optimized medium for P. cryoconitis BG5 was tested, and the observed optical density was 7.8. The cost-effectiveness of the optimized medium was determined as 6.25 unit prices per gram of cell produced in a 250-ml Erlenmeyer flask.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90985399","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
Editorial Board EOV 编辑委员会EOV
Preparative Biochemistry and Biotechnology Pub Date : 2015-11-17 DOI: 10.1080/10826068.2015.1018044
{"title":"Editorial Board EOV","authors":"","doi":"10.1080/10826068.2015.1018044","DOIUrl":"https://doi.org/10.1080/10826068.2015.1018044","url":null,"abstract":"","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91078347","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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