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    Bioprocess and Biosystems Engineering

    Bioprocess and Biosystems Engineering

    JournalISSN 1615-7591eISSN 1615-7605中科院 生物学 3区

    年发文量

    研究主题

    论文(4789)

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    1Bioleaching of Lithium from Lithium Refinery Residue Using A. Thiooxidans, A. Ferrooxidans, and a Mixed Culture of the Two Species
    Jia-li Huang, Zhi-gang Yin,Cheng-min Huang,Jin-yan Yang

    Lithium refinery residue (LRR), generated during the sulfuric acid processing of spodumene, is dominated by aluminosilicate phases and contains residual lithium (Li). Although bioleaching has been applied to primary Li ores and spent lithium-ion batteries, its applicability to aluminosilicate-dominated LRR remains poorly understood. Here, Acidithiobacillus thiooxidans, Acidithiobacillus ferrooxidans, and a mixed culture of the two species were evaluated for Li bioleaching from LRR. Among the conditions tested, the A. thiooxidans system achieved a Li leaching efficiency of 26.7

    2026
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    2Experimental Assessment of Sugar Losses and Energy Cost During Acid-Catalyzed Pretreatment of Sugarcane Bagasse at Low Solids Loading
    Yang Guo, Qingnan Zhu,Tao Han,Bin Zhang,Lixia Pan,Jie Bao

    Low solids loading is commonly applied in various pretreatment operations of lignocellulose biomass, especially for acid-catalyzed pretreatment. However, low solids loading condition inevitably leads to the generation of liquid streams containing considerable sugars and inhibitors. This study calculated the mass and energy balances for sulfuric acid-catalyzed pretreatment of sugarcane bagasse at a typical solids loading corresponding to a solid-to-liquid ratio of 1:20. A large volume of pretreatment liquor (18.5 g/g dry matter), which contained 27.4

    2026
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    3Proofing the Concept of a Segmented Biophotovoltaic Process to Produce Electricity from Marine Cyanobacteria: an Indoor and Outdoor Approach
    Giulia Evelin Oliveira Castro, Flavia Marisa Prado Saldanha-Correa, Guilherme Peixoto

    This study presents an innovative biophotovoltaic (BPV) process with three components: a cyanobacteria reservoir that serves as the biological engine; an electron-capture reactor that redirects transmembrane electrons; and a radiation-harvesting tower designed to maximize energy input and enhance system scalability. For the indoor (LED) and outdoor (solar radiation) tests, the most suitable resistances to yield the maximum current density were 164 Ω and 220 Ω, respectively. Indoor electricity generation peaked at 227 mW m− 2, with an average of 175 ± 47 mW m− 2, while outdoor tests peaked at 215 mW m− 2, with an average of 166 ± 26 mW m− 2, indicating similar efficiency under both conditions. To explain these efficiencies, the 5

    2026
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    4Integrated Dual Carbon Source and TCA Intermediate Supplementation in Fed-Batch Fermentation of CHO Cells for Reduced Lactate and Ammonia Accumulation and Improved IgG1 Monoclonal Antibody Titre
    Ashwin Naidu, Krutika Padhye, Prajakta Dandekar,Ratnesh Jain

    Chinese hamster ovary (CHO) cells are the workhorse of biopharmaceutical manufacturing, yet lactate and ammonia accumulation remain persistent bottlenecks that compromise cell viability, productivity, and product quality. To address this, we present an integrated feeding strategy systematically combining Ala-Gln, TCA intermediates, and glucose-galactose dual carbon feed evaluated head-to-head across four defined fed-batch conditions for CHO cultures producing an IgG1 monoclonal antibody (mAb). Conventional L-glutamine was replaced with L-alanyl-glutamine (Ala-Gln) to curb spontaneous ammonia release, while a customized “efficient feed mix” enriched with 2× TCA cycle intermediates and branched-chain amino acids combined with a glucose-galactose co-feed (2 mM glucose + 30 mM galactose) was introduced upon glucose depletion. Four fed-batch conditions were evaluated: a glutamine control (FB-01), Ala-Gln alone (FB-02), Ala-Gln with TCA intermediates (FB-03), and the complete integrated strategy (FB-04). FB-04 delivered an > 83

    2026
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    5Construction of an Industrial Host for the Efficient Active Expression of Protein Glutaminase (PG) in Bacillus Licheniformis
    Cuixia Zhou, Zhenyu Zhang,Kefen Wang, Wenlong Liu, Likun Wei, Yexue Liu

    Protein glutaminase (PG), a specific deaminase derived from C. proteolyticum, has been shown to hold significant potential for improving plant protein functionality. However, its industrial application is hindered by low expression level, inefficient activation from its proenzyme form (pro-PG), and high production costs in native or common heterologous hosts. To develop an effective industrial host for active expression of PG based on food-grade strain, the Bacillus licheniformis BL-LKT strain originated from enterprises was systematically modified and engineered. First, the extracellular polysaccharide (EPS) gene cluster was knocked out to alleviate cell aggregation, thereby enhancing cell growth and fermentation performance. Subsequently, a series of single and double knockout mutants of key extracellular protease genes (aprE, bpr, epr, vpr, wpr) were constructed to reduce the risk of PG hydrolysis by these proteases, while retaining sufficient proteolytic activity for pro-PG activation. The PG was then expressed in these engineered hosts using the shuttle vector pLY-3-PG. Among the constructed strains, the mutant EPE, which lacks eps, aprE, and epr, exhibited the highest PG activity of 0.537 U/mL, representing a 5.33-fold increase compared with the original strain. Fed-batch fermentation in a 5-L bioreactor ultimately yielded a PG activity of 2.35 U/mL, a 337.6

    2026
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    高被引作者

    作者引用发文
    Beom Soo Kim20559
    Jae Yong Song16622
    T. Panda139943
    de Oliveira Debora102735
    Sven-Olof Enfors101614
    Ho Nam Chang100620
    Dirk Weuster-Botz98328
    Sang Yup Lee95414
    Sung K Kim88323
    Michael Cotta8732

    高产作者

    作者引用发文
    T. Panda139943
    de Oliveira Debora102735
    Yuguo Zheng32830
    Helen Treichel72130
    Dirk Weuster-Botz98328
    Tony Hadibarata81725
    Sung K Kim88323
    Ju Chu33122
    Zhiqiang Liu21521
    Joaquim M. S. Cabral31520

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