Journal of Bioscience and Bioengineering

Publisher: Nihon Seibutsu Kogakkai, Elsevier

Journal description

Current impact factor: 1.79

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 1.79
2012 Impact Factor 1.737
2011 Impact Factor 1.793
2010 Impact Factor 1.707
2009 Impact Factor 1.749
2008 Impact Factor 1.702
2007 Impact Factor 1.782
2006 Impact Factor 1.136
2005 Impact Factor 0.948
2004 Impact Factor 0.802
2003 Impact Factor 0.993
2002 Impact Factor 0.777
2001 Impact Factor 0.865
2000 Impact Factor 0.749

Impact factor over time

Impact factor
Year

Additional details

5-year impact 1.99
Cited half-life 7.00
Immediacy index 0.29
Eigenfactor 0.01
Article influence 0.53
Other titles Journal of bioscience and bioengineering (En ligne)
ISSN 1347-4421
OCLC 56331911
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
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    • Deposit due to Funding Body, Institutional and Governmental policy or mandate only allowed where separate agreement between repository and the publisher exists.
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months .
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    • Published source must be acknowledged
    • Must link to journal home page or articles' DOI
    • Publisher's version/PDF cannot be used
    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: We developed two types of artificial platforms, T-junction and crossroad microchannel devices, and obtained guidance response ratio of pollen tubes to the female tissue as 56-57%. The crossroad device was also able to collect the attracted pollen tubes with high purity, which is useful for future omics analysis. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.03.021
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    ABSTRACT: This study investigates the biogas production from chicken manure at different organic loading rates (OLRs), in a mesophilic-thermophilic two stage anaerobic system. The system was operated on semi continuous mode under different OLRs [1.9 g volatile solids (VS)/L·d - 4.7 g VS/L·d] and total solid (TS) contents (3.0-8.25%). It was observed that the anaerobic bacteria acclimatized to high total ammonia nitrogen concentration (>3000 mg/L) originated as a result of the degradation of chicken manure. High volatile fatty acid concentrations were tolerated by the system due to high pH in the reactors. The maximum average biogas production rate was found as 554 mL/g VSfeed while feeding 2.2 g VS/L-d (2.3% VS - 3.8% TS) to the system. Average methane content of produced biogas was 74% during the study. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.01.021
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    ABSTRACT: The pla2 gene encoding a phospholipase A2 (EC 3.1.1.4) of Lactobacillus casei DSM20011 was cloned and expressed in the yeast Kluyveromyces lactis GG799 successfully for the first time. The structural pla2 gene fused in frame with the K. lactis secretion signal α-mating factor was integrated into the LAC4 locus and expressed under the control of the LAC4 promoter. sPLA2 activity was detected in the culture supernatant during shake flask culture of K. lactis/pKLAC1-pla2. In comparison with the control strain K. lactis/pKLAC1, SDS-PAGE analysis revealed a 17-kDa recombinant protein band in K. lactis/pKLAC1-pla2, which was consistent with the predicted molecular weight of the mature protein. Real-time quantitative PCR analysis indicated that the copy number of the integrated pla2 gene ranged from 2 to 6 and positively correlated with sPLA2 activity. When the inducer galactose was used as the carbon source, the sPLA2 activity in the culture supernatant of the recombinant that harbored six pla2 gene copies reached 1.96 ± 0.15 U/mL. The influence of the culture composition and conditions on the recombinant sPLA2 activity in shake flask culture were also studied. When the recombinant was cultured at 30°C in a YPD medium culture volume of 70 mL in a 250-mL shake flask with an initial pH of 7.0, the sPLA2 activity reached 2.16 ± 0.18 U/mL. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.03.022
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    ABSTRACT: The dihydrofolate reductase gene amplification system is widely used in Chinese hamster ovary (CHO) cells for the industrial production of therapeutic proteins. To enhance the efficiency of conventional gene amplification systems, we previously presented a novel method using cell-cycle checkpoint engineering. Here, we constructed high-producing and stable cells by the conditional expression of mutant cell division cycle 25 homolog B (CDC25B) using the Cre-loxP system. A bispecific antibody-producing CHO DG44-derived cell line was transfected with floxed mutant CDC25B. After inducing gene amplification in the presence of 250 nM methotrexate, mutant CDC25B sequence was removed by Cre recombinase protein expression. Overexpression of the floxed mutant CDC25B significantly enhanced the efficiency of transgene amplification and productivity. Moreover, the specific production rate of the isolated clone CHO Cre-1 and Cre-2 were approximately 11-fold and 15-fold higher than that of mock-transfected clone CHO Mock-S. Chromosomal aneuploidy was increased by mutant CDC25B overexpression, but Cre-1 and Cre-2 did not show any changes in chromosome number during long-term cultivation, as is the case with CHO Mock-S. Our results suggest that high-producing and stable cells can be constructed by conditionally controlling a cell-cycle checkpoint integrated in conventional gene amplification systems. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.04.009
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    ABSTRACT: This study aimed to optimize extracellular glutathione production by a Saccharomyces cerevisiae engineered strain and to concentrate the extracellular glutathione by membrane separation processes, including ultrafiltration (UF) and nanofiltration (NF). Synthetic defined (SD) medium containing 20 g L(-1) glucose was fermented for 48 h; the fermentation liquid was passed through an UF membrane to remove macromolecules. Glutathione in this permeate was concentrated for 48 h to 545.1 ± 33.6 mg L(-1) using the NF membrane; this was a significantly higher concentration than that obtained with yeast extract peptone dextrose (YPD) medium following 96 h NF concentration (217.9 ± 57.4 mg L(-1)). This higher glutathione concentration results from lower cellular growth in SD medium (final OD600 = 6.9 ± 0.1) than in YPD medium (final OD600 = 11.0 ± 0.6) and thus higher production of extracellular glutathione (16.0 ± 1.3 compared to 9.2 ± 2.1 mg L(-1) in YPD medium, respectively). Similar fermentation and membrane processing of sweet sorghum juice containing 20 g L(-1) total sugars provided 240.3 ± 60.6 mg L(-1) glutathione. Increased extracellular production of glutathione by this engineered strain in SD medium and subsequent UF permeation and NF concentration in shortend time may help realize industrial recovery of extracellular glutathione. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.05.013
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    ABSTRACT: This study was conducted to determine the effect of dietary supplement of bacterial lycopene (BL) produced by Escherichia coli on the egg quality and blood characteristics of laying quails. The antioxidant activity measurement showed that BL exhibited 100% 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging capacity at a concentration of 4.65 μg/ml, which was more effective than butylated hydroxytoluene (BHT) and commercial lycopene (CL). Moreover, seven dietary groups of laying quails consisting of 10 100-day-old quails (Coturnix coturnix japonica) each were fed with the basal diet supplemented with BL, CL or canthaxanthin (CA) for 4 weeks. Consequently, the triglyceride content of yolk was significantly lower in the group with BL and CL supplement. The serum malondialdehyde (MDA) level of the BL- and CA-supplemented groups at 18 mg/kg was lower than the control group. In conclusion, BL has a high antioxidant activity and is promising as a feed additive in the diet of laying quails. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.03.016
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    ABSTRACT: Chlorothalonil (CTN) is one of the most widely used fungicides and is often detected in the environment. Here, we report the isolation and characterization of a novel CTN-degrading bacterial strain XF-3 from long-term CTN-contaminated sites and identify it as a strain of the Paracoccus sp. The isolate could utilise CTN as the sole source of carbon and energy for growth. The optimal pH and temperature for degradation by XF-3 were 7.0 and 30°C, respectively. The CTN degradation gene was cloned by PCR. Although the results of a BLAST sequence search indicated that this gene has a 99% similarity with chd (a gene encoding the CTN hydrolytic dehalogenase), its hydrolytic efficiency for CTN was slightly greater than the chd from strain CTN-3. This is the first report of this gene from the genus Paracoccus. Therefore, there is a practical significance and a potential value of the isolated novel strain, XF-3. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.03.013
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    ABSTRACT: Embryoid body (EB) culture has been widely used for in vitro differentiation of embryonic stem (ES) cells. Micropatterning of cultures is a promising technique for regulating EB development, because it allows for controlling the EB size and the distance between neighboring EBs. In this study, we examined the relationship of EB separation distance to their growth and differentiation using a micropatterned chip. The basic chip design consisted of 91 gelatin spots (300 μm in diameter) in a hexagonal arrangement on a glass substrate that served as the cell adhesion area; the region without gelatin spots was modified with polyethylene glycol to create the non-adhesion area. Two similar chips were fabricated with distances between gelatin spots of 500 and 1500 μm. Mouse ES cells adhered on the gelatin spots and then proliferated to form EBs. When the EB-EB distance was at 1500 μm, their size and the expression of developmental gene markers were almost the same for all EBs on the chip. This indicated that interference between neighboring EBs was avoided. In contrast, when the EB-EB distance was at 500 μm, the size of EBs located in the inside region of the chip was smaller than that in the outside region. Additionally, in the inside region, hepatic differentiation of EB cells was increased over cardiac and vascular differentiation. These results indicate that the distance between EBs is an important factor in the regulation of their growth and differentiation. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 06/2015; DOI:10.1016/j.jbiosc.2015.04.018
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    ABSTRACT: We biosynthesized 6-deoxy-l-talose, 6-deoxy-l-sorbose, 6-deoxy-l-gulose, and 6-deoxy-l-idose, which rarely exist in nature, from l-fucose by coupling and sequential enzymatic reactions. The first product, 6-deoxy-l-talose, was directly produced from l-fucose by the coupling reactions of immobilized d-arabinose isomerase and immobilized l-rhamnose isomerase. In one-pot reactions, the equilibrium ratio of l-fucose, l-fuculose, and 6-deoxy-l-talose was 80:9:11. In contrast, 6-deoxy-l-sorbose, 6-deoxy-l-gulose, and 6-deoxy-l-idose were produced from l-fucose by sequential enzymatic reactions. d-Arabinose isomerase converted l-fucose into l-fuculose with a ratio of 88:12. Purified l-fuculose was further epimerized into 6-deoxy-l-sorbose by d-allulose 3-epimerase with a ratio of 40:60. Finally, purified 6-deoxy-l-sorbose was isomerized into both 6-deoxy-l-gulose with an equilibrium ratio of 40:60 by l-ribose isomerase, and 6-deoxy-l-idose with an equilibrium ratio of 73:27 by d-glucose isomerase. Based on the amount of l-fucose used, the production yields of 6-deoxy-l-talose, 6-deoxy-l-sorbose, 6-deoxy-l-gulose, and 6-deoxy-l-idose were 7.1%, 14%, 2%, and 2.4%, respectively. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 05/2015; DOI:10.1016/j.jbiosc.2015.04.017
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    ABSTRACT: The capacity of Trichoderma reesei cellulase to degrade lignocellulosic biomass has been enhanced by the construction of a recombinant T. reesei strain expressing Aspergillus aculeatus β-glucosidase I. We have confirmed highly efficient ethanol production from converge-milled Japanese cedar by recombinant T. reesei expressing A. aculeatus β-glucosidase I (JN11). We investigated the ethanol productivity of JN11 and compared it with the cocktail enzyme T. reesei PC-3-7 with reinforced cellobiase activity by the commercial Novozyme 188. Results showed that the ethanol production efficiency under enzymatic hydrolysis of JN11 was comparable to the cocktail enzyme both on simultaneous saccharification and fermentation (SSF) or separate hydrolysis and fermentation (SHF) processes. Moreover, the cocktail enzyme required more protein loading for attaining similar levels of ethanol conversion as JN11. We propose that JN11 is an intrinsically economical enzyme that can eliminate the supplementation of BGL for PC-3-7, thereby reducing the cost of industrial ethanol production from lignocellulosic biomass. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 05/2015; DOI:10.1016/j.jbiosc.2015.04.015
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    ABSTRACT: Long-term storage in aqueous solution has been demanded for the practical application of therapeutic proteins. Recently, a precipitation-redissolution method was proposed to prepare salt-dissociable protein-polyelectrolyte complex (PPC). To elucidate the utility of the complex for storage of proteins, we investigated the stress tolerance of PPC precipitates containing l-asparaginase (ASNase) and poly-l-lysine (polyK). PPC precipitate containing ASNase and polyK was prepared by precipitation-redissolution method. The sample was treated to three types of stress, i.e., heat, shaking, and oxidation. The protein concentration, enzyme activity, and CD spectrum of the supernatants of samples were measured after stressed. PPC precipitate consisting of ASNase and polyK showed tolerance against thermal and shaking stress compared to the native solution. In addition, PPC precipitate protected ASNase from inactivation by oxidation. PPC precipitate of ASNase/polyK complex successfully stabilized ASNase against physicochemical stresses. These results suggest that the PPC precipitate has great potential as a storage method in aqueous solution for unstable proteins. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 05/2015; DOI:10.1016/j.jbiosc.2015.04.010
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    ABSTRACT: Lantibiotics are antibacterial peptides containing unique thioether cross-links termed lanthionine and methyllanthionine. NukM, the modifying enzyme of nukacin ISK-1, which is produced by Staphylococcus warneri ISK-1, catalyzes the dehydration of specific Ser/Thr residues in a precursor peptide, followed by conjugative addition of intramolecular Cys to dehydrated residues to generate a cyclic structure. By contrast, the precursor peptide of nisin is modified by 2 enzymes, NisB and NisC, which mediate dehydration and cyclization, respectively. While the C-terminal domain of NukM is homologous to NisC, the N-terminal domain has no homology with other known proteins. We expressed and characterized the N- and C-terminal domains of NukM, NukMN, and NukMC, separately. In vitro reconstitution revealed that full-length NukM fully modified the substrate peptide NukA. NukMN partially phosphorylated, dehydrated, and cyclized NukA. By contrast, NukMC did not catalyze dehydration, phosphorylation, or cyclization reactions. Interaction studies using surface plasmon resonance analysis indicated that NukM and NukMN can bind NukA with high affinity, whereas NukMC has low substrate-recognition activity. These results suggest that NukMN is mainly responsible for substrate recognition and dehydration and that the whole NukM structure, including the C-terminal domain, is required for the complete modification of NukA. To the best of our knowledge, this is the first report providing insights into the in vitro catalytic activity of individual domains of a LanM-type modification enzyme. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 05/2015; DOI:10.1016/j.jbiosc.2015.03.020
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    ABSTRACT: Ophiostoma piceae secretes a versatile sterol-esterase (OPE) that shows high efficiency in both hydrolysis and synthesis of triglycerides and sterol esters. This enzyme produces aggregates in aqueous solutions, but the recombinant protein, expressed in Komagataella (synonym Pichia) pastoris, showed higher catalytic efficiency because of its higher solubility. This fact owes to a modification in the N-terminal sequence of the protein expressed in Pichia pastoris, which incorporated 4-8 additional amino acids, affecting its aggregation behavior. In this study we present a newly engineered P. pastoris strain with improved protein production. We also produced the recombinant protein in the yeast Saccharomyces cerevisiae and in the prokaryotic host Escherichia coli, corroborating that the presence of these N-terminal extra amino acids affected the protein's solubility. The OPE produced in the new P. pastoris strain presented the same physicochemical properties than the old one. An inactive form of the enzyme was produced by the bacterium, but the recombinant esterase from both yeasts was active even after its enzymatic deglycosylation, suggesting that the presence of N-linked carbohydrates in the mature protein is not essential for enzyme activity. Although the yield in S. cerevisiae was lower than that obtained in P. pastoris, this work demonstrates the importance of the choice of the heterologous host for successful production of soluble and active recombinant protein. In addition, S. cerevisiae constitutes a good engineering platform for improving the properties of this biocatalyst. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 05/2015; DOI:10.1016/j.jbiosc.2015.04.005
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    ABSTRACT: Three antigens (NcSAG1, NcSRS2 and NcMIC3) from Neospora caninum were expressed using the BmNPV bacmid system in silkworm larvae and purified from the hemolymph. From 20 silkworm larvae, 1.5, 1.2 and 1.4 mg of purified recombinant NcSAG1, NcSRS2 and NcMIC3 were obtained, respectively. When each purified recombinant antigen was immunized with Freund's incomplete adjuvant (FIA) to mice, recombinant NcSAG1 induced a Th2 immune response in immunized mice and produced a SAG1-specific antibody. In the experiment where NcSAG1-immunized mice were challenged with N. caninum, the cerebral N. caninum burden was significantly reduced compared with that of either the FIA- or PBS-immunized mice. Recombinant NcSRS2 or NcMIC3 induced both Th1 and Th2 immune responses, but NcMIC3-immunization did not induce significant production of NcMIC3-specific antibodies. These results suggest that the silkworm can produce recombinant antigens of N. caninum, which can be used as a recombinant vaccine against N. caninum. Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
    Journal of Bioscience and Bioengineering 04/2015; DOI:10.1016/j.jbiosc.2015.04.002
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    ABSTRACT: Transductions of exogenous proteins into cells enable the precise study of the effect of the transduced proteins on cellular functions. Accordingly, the protein transduction technique, which can control the release of proteins into the cytosol with certainty and high-throughput, is highly desired in various research fields. In this study, streptavidin (SA) labeled with a photosensitizer and cell-permeable peptides (CPP) was proposed as a nano-carrier for light-controlled protein transduction. SA was modified with biotinylated oligo-arginine peptides (Rpep), which were functionalized with Alexa Fluor 546 (AF546), to achieve cell penetrating and endosomal escape functionalities. The SA-Rpep complex was efficiently internalized into living HeLa cells corresponding to the length and the modification number of Rpep. SA conjugated with more than three equimolar AF546-modified Rpep consisting of fifteen arginine residues was achieved to diffuse throughout the cytosol without cytotoxicity by irradiation of the excitation light for AF546. The optimized nano-carrier was confirmed to transduce a biotinylated model cargo protein, enhanced green fluorescent protein fused with thioredoxin (tEGFP) into the cytosol at the light-irradiated area. The results provided proof-of-principle that SA possessing multiple AF546-modified Rpep has the potential to be a versatile and facile carrier for light-controlled protein transduction into the cytosol of mammalian cells. Copyright © 2015. Published by Elsevier B.V.
    Journal of Bioscience and Bioengineering 04/2015; 7. DOI:10.1016/j.jbiosc.2015.04.001