Preparative Biochemistry and Biotechnology最新文献_第2页

Kinetic characterization and fed-batch fermentation for maximal simultaneous production of esterase and protease from Lysinibacillus fusiformis AU01 梭状芽胞杆菌AU01产酯酶和蛋白酶的动力学特性及分批补料发酵

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1244685

K. Divakar, M. Suryia Prabha, G. Nandhinidevi, P. Gautam

{"title":"Kinetic characterization and fed-batch fermentation for maximal simultaneous production of esterase and protease from Lysinibacillus fusiformis AU01","authors":"K. Divakar, M. Suryia Prabha, G. Nandhinidevi, P. Gautam","doi":"10.1080/10826068.2016.1244685","DOIUrl":"https://doi.org/10.1080/10826068.2016.1244685","url":null,"abstract":"ABSTRACT The simultaneous production of intracellular esterase and extracellular protease from the strain Lysinibacillus fusiformis AU01 was studied in detail. The production was performed both under batch and fed-batch modes. The maximum yield of intracellular esterase and protease was obtained under full oxygen saturation at the beginning of the fermentation. The data were fitted to the Luedeking–Piret model and it was shown that the enzyme (both esterase and protease) production was growth associated. A decrease in intracellular esterase and increase in the extracellular esterase were observed during late stationary phase. The appearance of intracellular proteins in extracellular media and decrease in viable cell count and biomass during late stationary phase confirmed that the presence of extracellular esterase is due to cell lysis. Even though the fed-batch fermentation with different feeding strategies showed improved productivity, feeding yeast extract under DO-stat fermentation conditions showed highest intracellular esterase and protease production. Under DO-stat fed-batch cultivation, maximum intracellular esterase activity of 820 × 103 U/L and extracellular protease activity of 172 × 103 U/L were obtained at the 16th hr. Intracellular esterase and extracellular protease production were increased fivefold and fourfold, respectively, when compared to batch fermentation performed under shake flask conditions.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"38 1","pages":"323 - 332"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79393312","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: 4

Optimization of enzyme-assisted improvement of polyphenols and free radical scavenging activity in red rice bran: A statistical and neural network-based approach 酶辅助改善红米糠中多酚和自由基清除活性的优化:基于统计和神经网络的方法

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252926

Ashish A. Prabhu, A. Jayadeep

引用次数: 24

Enhanced production of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) copolymer and antimicrobial yellow pigmentation from Cupriavidus sp. USMAHM13 with antibiofilm capability 具有抗菌膜性能的Cupriavidus sp. usmama13聚(3-羟基丁酸酯-co-4-羟基丁酸酯)共聚物和抗菌黄色色素的增强生产

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252925

I. Ismail, Tana Poorani Gurusamy, H. Ramachandran, Abdullah Al-Ashraf Amirul

{"title":"Enhanced production of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) copolymer and antimicrobial yellow pigmentation from Cupriavidus sp. USMAHM13 with antibiofilm capability","authors":"I. Ismail, Tana Poorani Gurusamy, H. Ramachandran, Abdullah Al-Ashraf Amirul","doi":"10.1080/10826068.2016.1252925","DOIUrl":"https://doi.org/10.1080/10826068.2016.1252925","url":null,"abstract":"ABSTRACT Antibiofilm polymers have the ability to inhibit bacterial biofilm formation, which is known to occur ubiquitously in the environment and pose risks of infection. In this study, production of P(3HB-co-4HB) copolymer and antimicrobial yellow pigment from Cupriavidus sp. USMAHM13 are enhanced through medium optimization. Before the improvement of yellow pigment production, screening for the best additional supplement was performed resulting in high-yield yellow pigmentation using yeast extract with optimum concentration of 2 g/L. Effects of different concentrations of 1,4-butanediol, ammonium acetate, and yeast extract were studied using central composite design. Under optimal conditions, 53 wt% of polyhydroxyalkanoate (PHA) content, 0.35 g/L of pigment concentration, and 5.87 g/L of residual biomass were achieved at 0.56 wt% C of 1,4-butanediol, 1.14 g/L of ammonium acetate, and 2 g/L of yeast extract. Antibiofilm tests revealed that the yellow pigment coated on P(3HB-co-4HB) copolymer had significant effect on the inhibition of bacteria proliferation and colonization from 6 hr onward reaching 100% inhibition by 12 hr, hence effectively inhibiting the biofilm formation.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"384 1","pages":"388 - 396"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74964001","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: 4

Agricultural wastes as substrates for β-glucosidase production by Talaromyces thermophilus: Role of these enzymes in enhancing waste paper saccharification 农业废弃物作为嗜热Talaromyces生产β-葡萄糖苷酶的底物:这些酶在促进废纸糖化中的作用

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252928

Hanen Mallek-Fakhfakh, J. Fakhfakh, N. Masmoudi, Fatma Rezgui, A. Gargouri, H. Belghith

{"title":"Agricultural wastes as substrates for β-glucosidase production by Talaromyces thermophilus: Role of these enzymes in enhancing waste paper saccharification","authors":"Hanen Mallek-Fakhfakh, J. Fakhfakh, N. Masmoudi, Fatma Rezgui, A. Gargouri, H. Belghith","doi":"10.1080/10826068.2016.1252928","DOIUrl":"https://doi.org/10.1080/10826068.2016.1252928","url":null,"abstract":"ABSTRACT In the present study, we investigated a potent extracellular β-glucosidases secreted by the thermophilic fungal strain AX4 of Talaromyces thermophilus, isolated from Tunisian soil samples. This strain was selected referring to the highest thermostability of its β-glucosidases compared to the other fungal isolates. The β-glucosidase production was investigated by submerged fermentation. The optimal temperature and initial pH for maximum β-glucosidase production were 50°C and 7.0, respectively. Several carbon sources were assayed for their effects on β-glucosidase production, significant yields were obtained in media containing lactose 1% (3.0 ± 0.36 U/ml) and wheat bran 2% (4.0 ± 0.4 U/ml). The combination of wheat bran at 2% and lactose at 0.8% as carbon source enhanced β-glucosidase production, which reached 8.5 ± 0.28 U/ml. Furthermore, the β-glucosidase-rich enzymatic juice of T. thermophilus exhibited significant synergism with Trichoderma reesei (Rut C30) cellulases for pretreated waste paper (PWP) hydrolysis. Interestingly, the use of this optimal enzymatic cocktail increased 4.23 fold the glucose yield after saccharification of waste paper. A maximum sugar yield (94%) was reached when using low substrate (2%) and enzyme loading (EC1).","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"80 1","pages":"414 - 423"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87219466","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: 11

Production, characterization, and immobilization of partially purified surfactant–detergent and alkali-thermostable protease from newly isolated Aeromonas caviae 新分离的气单胞菌部分纯化表面活性剂-清洁剂和碱耐热蛋白酶的制备、表征和固定化

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1244688

Sumitra Datta, G. Menon, Bincy Varughese

{"title":"Production, characterization, and immobilization of partially purified surfactant–detergent and alkali-thermostable protease from newly isolated Aeromonas caviae","authors":"Sumitra Datta, G. Menon, Bincy Varughese","doi":"10.1080/10826068.2016.1244688","DOIUrl":"https://doi.org/10.1080/10826068.2016.1244688","url":null,"abstract":"ABSTRACT Proteolytic Aeromonas caviae P-1-1 growing at wide-ranging pH (7.0–11.0) and moderate salinity (0–5% NaCl) was isolated from cattle shed of Thanjavur, India. It produced lipase, gelatinase, and polyhydroxybutyrate. Different culture conditions, incubation time, carbon and nitrogen sources, vitamins, amino acids, surfactants, and metal ions for optimal growth and protease production of P-1-1 were examined. Maximum protease (0.128 U/mL) production was achieved with 1% fructose, 1% yeast extract, 0.1% ammonium sulfate, 3% NaCl, 0.1% CaCl2 · 2H2O, 1% glycine, 0.1% vitamin E, and 0.1% Tween-40 at pH 8.0 after 42 hr of incubation at 37°C. It was active over broad range of pH (7.0–12.0), temperature (15–100°C), and salinity (0–9% NaCl) with optima at pH 10.0, 55°C, and 3% NaCl. It retained 65 and 48% activities at pH 12.0 and 100°C, respectively. Partially purified protease was highly stable (100%) within pH range 7.0–12.0 and salinities of 0–5% NaCl for 48 hr. Cu2+, Mn2+, Co2+, and Ca2+ did not inhibit its activity. Its stability at extreme pHs, temperatures, and in the presence of surfactants and commercial detergents suggests its possible application in laundry detergents. Partially purified protease was immobilized and reused. This is the first report of alkali-thermotolerant, surfactant–detergent-stable partially purified extracellular protease from A. caviae.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"40 1","pages":"349 - 356"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81299981","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: 8

X-ray-induced mutation of Bacillus sp. MR10 for manno-oligosaccharides production from copra meal x射线诱导芽孢杆菌MR10突变从椰粕中生产甘露寡糖

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252929

S. Chaikaew, Apinun Kanpiengjai, Jenjira Intatep, Kridsada Unban, P. Wongputtisin, Goro Takata, C. Khanongnuch

{"title":"X-ray-induced mutation of Bacillus sp. MR10 for manno-oligosaccharides production from copra meal","authors":"S. Chaikaew, Apinun Kanpiengjai, Jenjira Intatep, Kridsada Unban, P. Wongputtisin, Goro Takata, C. Khanongnuch","doi":"10.1080/10826068.2016.1252929","DOIUrl":"https://doi.org/10.1080/10826068.2016.1252929","url":null,"abstract":"ABSTRACT The present study demonstrates the effectiveness of X-ray radiation in strain improvement for defective lipase production by Bacillus sp. MR10 for further application in the fermentative production of manno-oligosaccharides (MOS) from agricultural by-product, defatted copra meal (DCM). The mutants obtained were screened based on their defective lipase activity together with their β-mannanase production performance. Among 10 selected mutants, the strain M7 was the highest promising mutant regarding the smallest lipase activity (0.05 U/ml) and the retained β-mannanase activity similar to the parental strain (22 U/ml) were detected. The mutant M7 effectively hydrolyzed DCM to MOS with low-degree of polymerization (DP) oligomers including mannotriose (M3), mannotetraose (M4), and mannopentose (M5) as the main products. Although the pattern of DCM hydrolysis products of mutant M7 was distinctly different from wild type, the biochemical and catalytic properties of purified β-mannanase of mutant were similar to those of wild type. Both purified β-mannanases with apparent molecular mass of 38 kDa displayed optimal activity at pH 5–7 and 45–55°C. Co2+ and Hg2+ nearly completely inhibited activities of both enzymes, whereas Ba2+, Fe3+, and 2-mercaptoethanol obviously activated enzyme activities. Both enzymes showed high specificity for locust bean gum, konjac mannan, DCM, and guar gum. Thus, the mutant M7 has a potential for commercial production of high-quality MOS from low-cost DCM for further application in the feed industry.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"26 1","pages":"424 - 433"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86053314","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: 5

Production of nanocellulose in miniature-bioreactor: Optimization and characterization 微型生物反应器生产纳米纤维素:优化与表征

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252923

Sepideh Khazeni, A. Hatamian-Zarmi, F. Yazdian, Z. Mokhtari-Hosseini, B. Ebrahimi-Hosseinzadeh, Behnam Noorani, Ghassem Amoabedini, M. Soudi

引用次数: 6

Optimization of recombinant β-NGF expression in Escherichia coli using response surface methodology 利用响应面法优化重组β-NGF在大肠杆菌中的表达

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252927

Pouria Gholami Tilko, Z. Hajihassan, H. Moghimi

{"title":"Optimization of recombinant β-NGF expression in Escherichia coli using response surface methodology","authors":"Pouria Gholami Tilko, Z. Hajihassan, H. Moghimi","doi":"10.1080/10826068.2016.1252927","DOIUrl":"https://doi.org/10.1080/10826068.2016.1252927","url":null,"abstract":"ABSTRACT Human nerve growth factor a member of the neurotrophin family can be used to treat neurodegenerative diseases. As it has disulfide bonds in its structure, periplasmic expression of it using appropriate signal sequence is beneficial. Therefore, in this work β-nerve growth factor (β-NGF) was expressed in Escherichia coli using pET39b expression vector containing DsbA signal sequence. In an initial step, the effect of isopropyl β-D-1-thiogalactopyranoside (IPTG) and lactose concentration as inducer on protein production was investigated using response surface methodology. Then the effect of different postinduction time and temperature on protein production was studied. Our results indicated that the highest β-NGF production was achieved with 1 mM IPTG and low concentrations of lactose (0–2% w/v), low cultivation temperature of 25°C and postinduction time of 2 hr. Also following β-NGF purification, bioassay test using PC12 cell line was done. The biological activity of the purified β-NGF showed a similar cell proliferation activity with the standard recombinant human β-NGF. In conclusion, the results indicated an optimized upstream process to obtain high yields of biologically active β-NGF.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"27 1","pages":"406 - 413"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79153863","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: 8

Enhancing granulocyte colony-stimulating factor expression in Pichia pastoris through fusion with human serum albumin 通过与人血清白蛋白融合增强毕赤酵母中粒细胞集落刺激因子的表达

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1252922

Moolchand Sigar, N. Maity, S. Mishra

{"title":"Enhancing granulocyte colony-stimulating factor expression in Pichia pastoris through fusion with human serum albumin","authors":"Moolchand Sigar, N. Maity, S. Mishra","doi":"10.1080/10826068.2016.1252922","DOIUrl":"https://doi.org/10.1080/10826068.2016.1252922","url":null,"abstract":"ABSTRACT Protein fusion technology has emerged as one of the important strategies to increase the level of expression and half-life of therapeutic proteins in heterologous expression systems. Granulocyte colony-stimulating factor (G-CSF) is a hematopoietic growth factor and is clinically used against neutropenia. Enhanced expression and stability of G-CSF were achieved in Pichia pastoris by the way of constructing a fusion protein with human serum albumin (HSA). The strategy involved polymerase chain reaction (PCR) amplification of fragments corresponding to codon-optimized G-CSF and domain 3 of HSA. Overlapping PCR was used to obtain the full-length fused gene (1,184 bp) with a 15-bp linker sequence comprising of 4 Gly and 1 Ser residues. Extracellular expression was carried out downstream of α-factor secretion signal sequence under the control of alcohol oxidase 1 promoter using pPICZαB. Excreted protein in the range of 110–380 mg L−1 was observed among the transformants. Effect of aeration and temperature was investigated in one of the transformants (35) overexpressing fusion protein and levels of G-CSF enhanced by 1.8-fold and 2.3-fold, respectively. Assay of biological activity indicated the fusion protein to retain similar cell proliferation activity as the commercial G-CSF preparation.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"35 1","pages":"364 - 370"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78393524","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: 11

Single temperature liquefaction process at different operating pHs to improve ethanol production from Indian rice and corn feedstock 不同操作ph下的单温度液化工艺以提高印度大米和玉米原料的乙醇产量

Preparative Biochemistry and Biotechnology Pub Date : 2017-04-21 DOI: 10.1080/10826068.2016.1244687

V. Gohel, K. Ranganathan, G. Duan

{"title":"Single temperature liquefaction process at different operating pHs to improve ethanol production from Indian rice and corn feedstock","authors":"V. Gohel, K. Ranganathan, G. Duan","doi":"10.1080/10826068.2016.1244687","DOIUrl":"https://doi.org/10.1080/10826068.2016.1244687","url":null,"abstract":"ABSTRACT Conventional grain ethanol manufacturing is a high-temperature energy-intensive process comprising of multiple-unit operations when combined with lower ethanol recovery results in higher production cost. In liquefaction, jet cooking accounts for significant energy cost, while strong acid or base used for pH adjustment presents a safety hazard. A need is felt for sustainable ethanol manufacturing process that is less hazardous, consumes lower energy, and operates in a low pH range of 4.50–5.50. A single temperature liquefaction (STL) process that could efficiently operate at lower liquefaction temperature over a pH range of 4.50–5.50 was developed using rice and corn feedstock. Ethanol recovery witnessed at pH 4.5, 5.0, and 5.5 are 481.2 ± 1.5, 492.4 ± 1.5, and 493.6 ± 1.5 L MT−1 rice, respectively. Similarly, ethanol recovery witnessed at pH 4.5, 5.0, and 5.5 are 404.6 ± 1.3, 413.9 ± 0.8, and 412.4 ± 1.8 L MT−1 corn, respectively. The improvement in ethanol recovery is attributed to higher starch conversion by alpha-amylase even at pH as low as 4.50. Thus, the STL process operated at pH lower than 5.20 is poised to enhance sustainability by offering dual advantage of energy as well as chemical saving.","PeriodicalId":20393,"journal":{"name":"Preparative Biochemistry and Biotechnology","volume":"159 1","pages":"342 - 348"},"PeriodicalIF":0.0,"publicationDate":"2017-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75114762","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