Process Biochemistry最新文献

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The effect of Echinacea purpurea polysaccharide on gut microbiota and serum metabolism in Lewis lung cancer mice
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2025-01-08 DOI: 10.1016/j.procbio.2025.01.005
Jian Shen , Changhui Du , Fanglin Shen , Qichen Cui , He Qian , Yong Zhao
{"title":"The effect of Echinacea purpurea polysaccharide on gut microbiota and serum metabolism in Lewis lung cancer mice","authors":"Jian Shen ,&nbsp;Changhui Du ,&nbsp;Fanglin Shen ,&nbsp;Qichen Cui ,&nbsp;He Qian ,&nbsp;Yong Zhao","doi":"10.1016/j.procbio.2025.01.005","DOIUrl":"10.1016/j.procbio.2025.01.005","url":null,"abstract":"<div><div>Lung cancer is closely associated with chronic inflammation and metabolic dysregulation, which contribute to tumor progression and pose significant challenges for effective treatment. <em>Echinacea purpurea</em> polysaccharide (EP) can regulate immunity and gut microbiota, but its specific impact on lung cancer through gut microbiota or its broader metabolic effects remains underexplored. This study aims to investigate the intervention effect of EP on lung cancer and its impact on gut microbiota and metabolism. The tumor inhibition rate of EP was 46.7 %, and it could downregulate the expression level of Ki67 protein in tumor tissues, reduce the level of inflammation and growth factors. The intervention of EP preserved intestinal barrier integrity and increased the level of beneficial microbiota, such as <em>Blautia</em>, <em>Faecalibaculum</em>, and <em>Dubosiella</em>, associated with the production of short-chain fatty acids (SCFAs). Furthermore, the different metabolites showed that EP primarily impacted amino acid metabolism, lipid metabolism and carbohydrate metabolism pathways. The correlation analysis showed that EP could affect the serum metabolic pathways through the gut microbiota. Meanwhile, EP transmitted anti-inflammatory and anti-angiogenic signals, regulated the immune environment, thus preventing the onset and development of lung cancer. This suggests that EP could be an adjuvant in lung cancer prevention and treatment strategies.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 121-133"},"PeriodicalIF":3.7,"publicationDate":"2025-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Dual cross-linked hydrogel microbial reactor: An improved microbial immobilization technology to treat mixed electroplating wastewater
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2025-01-08 DOI: 10.1016/j.procbio.2025.01.001
Jiali Song , Binbin Ran , Qiang An , Shuman Deng , Zige Feng , Bin Zhao , Weifeng Zhang
{"title":"Dual cross-linked hydrogel microbial reactor: An improved microbial immobilization technology to treat mixed electroplating wastewater","authors":"Jiali Song ,&nbsp;Binbin Ran ,&nbsp;Qiang An ,&nbsp;Shuman Deng ,&nbsp;Zige Feng ,&nbsp;Bin Zhao ,&nbsp;Weifeng Zhang","doi":"10.1016/j.procbio.2025.01.001","DOIUrl":"10.1016/j.procbio.2025.01.001","url":null,"abstract":"<div><div>In this study, the microbial immobilization technology has been effectively improved and applied to the treatment of mixed electroplating wastewater. The hydrogel beads embedding peanut shell biochar (PBC) and <em>Pseudomonas hibiscicola</em> strain L1 (strain L1) were prepared by polyvinyl alcohol (PVA) and sodium alginate (SA). Response surface methodology (RSM) was used to optimize the preparation of hydrogel beads, and the optimal conditions were as follows: PBC: 3.26 % (w/v), SA: 1.75 % (w/v), PVA: 7.62 % (w/v). The composites showed a significant increase in wastewater treatment capacity compared that without biochar addition. The optimum removal of pollutants in sequencing batch reactor (SBR) was Ni(II): 79.59 %, Cr(VI): 55.30 %, Cu(II): 83.72 %, Zn(II): 87.09 % and ammonia nitrogen: 74.56 %. Scanning electron microscopy (SEM) results showed that the material had a dense reticulated internal structure and produced a large number of microbial metabolic deposits. Fourier transform infrared spectroscopy (FTIR) detected that the material contained various functional groups such as -OH, -CHO, C<img>O, PO<sub>4</sub><sup>3-</sup> and C-H; X-ray diffraction (XRD) analysis showed that crystals of Ni<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub>·8 H<sub>2</sub>O, CrPO<sub>4</sub>, Cr(OH)<sub>3</sub>·3 H<sub>2</sub>O, CuCO<sub>3</sub>, Zn(OH)<sub>2</sub>, and Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> were formed on the surface of the material. The structure remained intact and still maintained some microbial activity after seven cycles. Therefore, the material prepared has a broad potential in the treatment of mixed electroplating wastewater.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 57-67"},"PeriodicalIF":3.7,"publicationDate":"2025-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Potential of plants-based alkaloids, terpenoids and flavonoids as antibacterial agents: An update
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2025-01-05 DOI: 10.1016/j.procbio.2025.01.003
Ankumoni Das, Rohit Ruhal
{"title":"Potential of plants-based alkaloids, terpenoids and flavonoids as antibacterial agents: An update","authors":"Ankumoni Das,&nbsp;Rohit Ruhal","doi":"10.1016/j.procbio.2025.01.003","DOIUrl":"10.1016/j.procbio.2025.01.003","url":null,"abstract":"<div><div>Antimicrobial resistance (AMR) has emerged as a critical public health concern in the 21st century, driven by the overuse and misuse of antibiotics. This review focuses on the potential of phytochemicals, notably flavonoids, terpenoids, and alkaloids, as alternative antibacterial agents to treat resistant pathogens. These natural chemicals have a variety of chemical compositions and modes of action that can suppress bacterial growth while increasing the efficiency of current antibiotics. Phytochemicals have been demonstrated to target numerous pathways within bacterial cells, lowering the chances of resistance development. Despite their potential, there is still a significant gap in knowing how to successfully employ these chemicals for therapeutic purposes. The study underlines the necessity for novel research approaches for looking into phytochemicals' antibacterial capabilities and synergistic effects with conventional antibiotics. By resolving these gaps, the scientific community can unleash the therapeutic potential of plant-derived compounds, revealing the path for new approaches to combating AMR and improving public health outcomes. This compilation of existing information intends to stimulate further research into the use of phytochemicals in current medicine, ultimately helping to combat antibiotic-resistant pathogens.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 94-120"},"PeriodicalIF":3.7,"publicationDate":"2025-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099613","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Understanding selenoproteins: Structural insights, biological functions and transformative applications in therapeutics
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2025-01-03 DOI: 10.1016/j.procbio.2024.12.028
Bhairav Prasad , Akanksha Akanksha , Palki Sahib Kaur , Saurabh Gupta
{"title":"Understanding selenoproteins: Structural insights, biological functions and transformative applications in therapeutics","authors":"Bhairav Prasad ,&nbsp;Akanksha Akanksha ,&nbsp;Palki Sahib Kaur ,&nbsp;Saurabh Gupta","doi":"10.1016/j.procbio.2024.12.028","DOIUrl":"10.1016/j.procbio.2024.12.028","url":null,"abstract":"<div><div>Present study summarizes the key role of selenoproteins in biological processes, their therapeutic potential, and the implications of their dysfunction in various diseases. Selenoproteins play a vital role in various biological functions, including antioxidative defense, thyroid hormone metabolism, and redox balance maintenance. These proteins are critical for immune responses, muscle development, and cellular integrity. Sophisticated techniques like X-ray crystallography and mass spectrometry have been used to characterize their structures and interactions. Selenoproteins have promising applications in medicine as therapeutic agents and nutritional supplements for cancer, cardiovascular disorders, immune function, mitochondrial health, and neurodegenerative diseases. Deficiencies in dietary selenium or mutations in selenoproteins can lead to disorders such as cancer, Kashin-Beck disease, Keshan disease, atherosclerosis, and DNA damage. This review covers the occurrence, diversity, biological roles, and therapeutic potential of selenoproteins in health and disease. In conclusion, selenoproteins are essential for maintaining cellular homeostasis and overall health, with their diverse biological roles, therapeutic potential, and association with various diseases. Future research should focus on further elucidating the molecular mechanisms underlying selenoprotein function, optimizing their therapeutic applications, and exploring novel strategies for preventing and treating selenoprotein-related diseases.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 148-160"},"PeriodicalIF":3.7,"publicationDate":"2025-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099610","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Oceanobacillus in high-temperature Daqu: Taxonomic diversity, metabolic characteristics and biofortification effect
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2025-01-02 DOI: 10.1016/j.procbio.2025.01.002
Xu Liu , Jun-Jie Fu , Han-Jun Shen , Li-Juan Chai , Xiao-Juan Zhang , Hong-Yu Xu , Song-Tao Wang , Su-Yi Zhang , Cai-Hong Shen , Jin-Song Shi , Zhen-Ming Lu , Zheng-Hong Xu
{"title":"Oceanobacillus in high-temperature Daqu: Taxonomic diversity, metabolic characteristics and biofortification effect","authors":"Xu Liu ,&nbsp;Jun-Jie Fu ,&nbsp;Han-Jun Shen ,&nbsp;Li-Juan Chai ,&nbsp;Xiao-Juan Zhang ,&nbsp;Hong-Yu Xu ,&nbsp;Song-Tao Wang ,&nbsp;Su-Yi Zhang ,&nbsp;Cai-Hong Shen ,&nbsp;Jin-Song Shi ,&nbsp;Zhen-Ming Lu ,&nbsp;Zheng-Hong Xu","doi":"10.1016/j.procbio.2025.01.002","DOIUrl":"10.1016/j.procbio.2025.01.002","url":null,"abstract":"<div><div>High-temperature Daqu (HTD) is a critical component in Jiang-flavor Baijiu production, supplying flavor precursors, enzymes, and diverse microorganisms. Notably, HTD harbors <em>Oceanobacillus</em>, an ecological generalist whose role in the microecosystem remains to be defined. Here, we first identified 21 amplicon sequence variants (ASVs) belonging to six <em>Oceanobacillus</em> species in 20 HTD samples through 16S rRNA gene sequencing. Subsequently, representative strains of eight <em>Oceanobacillus</em> species were selectively isolated from HTD using predicted culture media. These strains exhibited potent enzymatic activities including cellulase and neutral proteinase, alongside diverse metabolic capabilities. Furthermore, we evaluated the impact of <em>Oceanobacillus caeni</em>, the predominant species, on HTD fermentation. Compared to the control, the relative abundance of <em>Oceanobacillus caeni</em> in the biofortified HTD increased significantly, from 3.82 % to 10.25 %, with the biomass of <em>Oceanobacillus caeni</em> surged from 5.15 × 10<sup>8</sup> to 2.95 × 10<sup>9</sup> copies/g. The activities of cellulase and neutral proteinase in the biofortified HTD escalated to 1.20 U and 57.14 U, respectively. The levels of volatile pyrazines and phenols in the biofortified HTD increased by 1.45 and 1.55 times, respectively. Levels of other volatiles including isovaleraldehyde, furfural, isobutyric acid, phenylacetone, ethyl palmitate, and 1,2-dimethoxybenzene saw respective increases of 3.77, 2.26, 1.94, 2.21, 5.21, and 2.27 times. This study sheds light on the role of <em>Oceanobacillus</em> in HTD, offering a theoretical foundation for improving Daqu quality.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 68-79"},"PeriodicalIF":3.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Direct immobilization of an engineered Bacillus subtilis lipase A variant: Evaluation of substrate specificity, solvent stability and peptide synthesis
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2024-12-31 DOI: 10.1016/j.procbio.2024.12.027
Karen Rodríguez-Núñez , Manuel Barraza , Pamela Vásquez , Claudia Bernal , Ronny Martínez
{"title":"Direct immobilization of an engineered Bacillus subtilis lipase A variant: Evaluation of substrate specificity, solvent stability and peptide synthesis","authors":"Karen Rodríguez-Núñez ,&nbsp;Manuel Barraza ,&nbsp;Pamela Vásquez ,&nbsp;Claudia Bernal ,&nbsp;Ronny Martínez","doi":"10.1016/j.procbio.2024.12.027","DOIUrl":"10.1016/j.procbio.2024.12.027","url":null,"abstract":"<div><div>Enzyme-mediated peptide synthesis is a promising alternative for current industrial requirements, mainly due to its potential for increasing process sustainability and efficiency. In this work, peptide synthesis using lipases was studied, and the peptide synthesis activity of a previously reported <em>Bacillus subtilis</em> lipase A (BSLA) variant, P5F3_BSLA (F41L-∆W42-∆D43-R44P) was evaluated. P5F3_BSLA was immobilized on a hydrophilic mesoporous silica support functionalized with glyoxyl groups. A rapid and direct immobilization approach was used from cell culture supernatant in a single vessel without prior protein purification. The effect of immobilization on the performance of P5F3_BSLA regarding substrate specificity, peptide synthesis, and thermal and solvent resistance was evaluated and compared to the WT_BSLA enzyme. The variant showed a similar immobilization yield compared to Wt_BSLA; however, it showed different immobilization kinetics. The P5F3 variant showed an increased solvent resistance in 100 % isopropyl alcohol and an increased activity against long-chain fatty acid substrates. Besides, the P5F3_BSLA variant showed a 1.2-fold increase in glycine polymerization compared to WT_BSLA. The simple, efficient, and successful immobilization of this lipase, its resistance to solvents, and its potential use in peptide synthesis opens an exciting possibility of applications for the industry, highlighting the combination of protein engineering and enzyme immobilization tools to develop biocatalysts with novel properties from widely studied enzymes.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 49-56"},"PeriodicalIF":3.7,"publicationDate":"2024-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Prospective comparison between mannan-oligosaccharide (MOS) and other hemicellulose-derived oligosaccharides
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2024-12-31 DOI: 10.1016/j.procbio.2024.12.026
Nadinne Medeiros Assis , Viridiana Santana Ferreira-Leitão , Ayla Sant’Ana da Silva
{"title":"Prospective comparison between mannan-oligosaccharide (MOS) and other hemicellulose-derived oligosaccharides","authors":"Nadinne Medeiros Assis ,&nbsp;Viridiana Santana Ferreira-Leitão ,&nbsp;Ayla Sant’Ana da Silva","doi":"10.1016/j.procbio.2024.12.026","DOIUrl":"10.1016/j.procbio.2024.12.026","url":null,"abstract":"<div><div>Mannan-oligosaccharides (MOS) are emerging prebiotics composed of mannose residues linked by α- or β-glycosidic bonds. α-MOS are derived from the cell wall of <em>Saccharomyces cerevisiae</em>, while β-MOS can be derived from mannan-rich plants, offering a sustainable approach to obtaining byproducts. To understand the landscape of β-MOS production, this study compares α-MOS and β-MOS with other plant-based oligosaccharides, including xylo-oligosaccharides (XOS) and arabino-(xylan)-oligosaccharides (AOS/AXOS), through scientific, technological, and market surveys. The analysis revealed growing interest in XOS, followed by MOS, and early stages of R&amp;D in AOS/AXOS. Manual curation of MOS studies indicated that β-MOS production is concentrated on sources like konjac and carob, with increasing attention on agro-residues from coffee, coconut, and oil palm industries. The production process often involves enzymatic hydrolysis, highlighting biotechnology's role. The market shows established α-MOS products and the rise of β-MOS. This study identifies research gaps and market opportunities for hemicellulose-derived oligosaccharides, particularly β-MOS.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 33-48"},"PeriodicalIF":3.7,"publicationDate":"2024-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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 novel dual-function biomimetic approach for high throughput organic dye biodegradation and hydrogen peroxide sensing using a nanosized artificial peroxidase with ultra-improved substrate affinity and superb catalytic efficiency
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2024-12-28 DOI: 10.1016/j.procbio.2024.12.025
Saeed Reza Hormozi Jangi , Zahra Dehghani
{"title":"A novel dual-function biomimetic approach for high throughput organic dye biodegradation and hydrogen peroxide sensing using a nanosized artificial peroxidase with ultra-improved substrate affinity and superb catalytic efficiency","authors":"Saeed Reza Hormozi Jangi ,&nbsp;Zahra Dehghani","doi":"10.1016/j.procbio.2024.12.025","DOIUrl":"10.1016/j.procbio.2024.12.025","url":null,"abstract":"<div><div>A high throughput novel dual-function biomimetic artificial enzyme-based approach was developed for dye biodegradation and hydrogen peroxide quantification using a nanosized artificial peroxidase with superb catalytic efficiency and ultra-improved substrate affinity compared to the native enzyme. The artificial peroxidase was chemically, kinetically, and biochemically characterized. A high specific activity of 0.0503 UI mg<sup>−1</sup>, an optimal-pH of 4.0, an optimal-temperature of 35 ℃, and a high storage stability for at-least 30 days was determined for this nanozyme. It retained 88.2 % and 90 % of its activity at 60 ℃ (200 min) and 5 cycles, respectively, revealing its high thermal and cycling stability. Its catalytic efficiency and substrate affinity were 3.2-fold and 7.1-order higher than the native peroxidase, respectively. The mechanistic insights were provided for the activity of nanozyme. A dye biodegrading protocol with a yield of 99.1 % (75.2 % after 10 reuses) within 30.0 min was developed and applied for dye degradation from real waters and textile wastewater. An analytical highly sensitive, reproducible, and selective H<sub>2</sub>O<sub>2</sub> biosensor was also designed, providing a linear quantification range over 1.0–180.0 µM, a detection limit of 0.23 µM, and accurate results for milk analysis. This method showed very better figures of merits than reported ones.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 1-20"},"PeriodicalIF":3.7,"publicationDate":"2024-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Sustainable production of polyhydroxybutyrate biopolymers and cellulose microfibers from sugarcane waste
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2024-12-25 DOI: 10.1016/j.procbio.2024.12.022
Treerat Sooksawat , Ketsaraporn Ngaopok , Surasak Siripornadulsil , Sittipong Amnuaypanich , Marisa Attapong , Wilailak Siripornadulsil
{"title":"Sustainable production of polyhydroxybutyrate biopolymers and cellulose microfibers from sugarcane waste","authors":"Treerat Sooksawat ,&nbsp;Ketsaraporn Ngaopok ,&nbsp;Surasak Siripornadulsil ,&nbsp;Sittipong Amnuaypanich ,&nbsp;Marisa Attapong ,&nbsp;Wilailak Siripornadulsil","doi":"10.1016/j.procbio.2024.12.022","DOIUrl":"10.1016/j.procbio.2024.12.022","url":null,"abstract":"<div><div>Thermochemically pretreating sugarcane bagasse (SCB) and sugarcane leaves (SCL) at 121 °C generated fermentable sugars that were transformed into polyhydroxybutyrate (PHB) by PHB-producing bacteria. The SCB hydrolysate contained reducing sugars (25.0–26.1 g/L), which were mainly xylose (16.4–17.6 g/L) and glucose (7.8–8.0 g/L). The bacteria used glucose more effectively than xylose and glycerol did, as the maximum PHB contents (% cell dry weight) observed with glucose, xylose, and glycerol were 69.3 %, 16.2 %, and 21.4 %, respectively. After 72 h of incubation, <em>Burkholderia cepacia</em> ASL22 and <em>Priestia megaterium</em> ASL11, KKR5, and SRB3 converted 50 % of the SCB hydrolysate in E2 broth into PHB, and the maximum weight (1.97 g/L) and content (32.6 %) of PHB were obtained with <em>B. cepacia</em> ASL22. Strain ASL22 also grew on E2 agar, producing 56.0 g/L PHB when 10 % SCB hydrolysate and 0.3 % (v/v) glycerol were used as cosubstrates. Furthermore, combining alkaline treatment, xylanase hydrolysis, and NaClO<sub>2</sub> bleaching converted SCB and SCL into high-purity cellulose microfibers (CMF) with a low yield (31 %). After peroxide bleaching, alkaline treatment and sonication, the CMF yields ranged from 88.3 % to 95.1 %, but some lignin and hemicellulose remained. Thus, sugarcane waste can be processed biologically and physicochemically to produce value-added products, thereby reducing pollution.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 134-147"},"PeriodicalIF":3.7,"publicationDate":"2024-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
Designing a cost-effective and scalable expression platform for highly efficient recombinant endo-β-N-acetylglucosaminidase H using fed-batch strategy in E. coli
IF 3.7 3区 生物学
Process Biochemistry Pub Date : 2024-12-24 DOI: 10.1016/j.procbio.2024.12.019
Shilpa Mohanty, Babbal, Mohini Talwar, Shivani Chauhan, Priya Sinha, Shubham Sharma, Yogender Pal Khasa
{"title":"Designing a cost-effective and scalable expression platform for highly efficient recombinant endo-β-N-acetylglucosaminidase H using fed-batch strategy in E. coli","authors":"Shilpa Mohanty,&nbsp;Babbal,&nbsp;Mohini Talwar,&nbsp;Shivani Chauhan,&nbsp;Priya Sinha,&nbsp;Shubham Sharma,&nbsp;Yogender Pal Khasa","doi":"10.1016/j.procbio.2024.12.019","DOIUrl":"10.1016/j.procbio.2024.12.019","url":null,"abstract":"<div><div><em>N</em>-glycosylation of proteins is a complex post-translational phenomenon critical in key cellular processes. Anomalies in protein glycosylation leads to the onset of disease. Therefore, it necessitates stringent monitoring of glycosylation patterns in recombinant proteins as the <em>N</em>-glycans modulate their pharmacokinetics, stability, activity, and immunogenicity. <em>N-</em>glycans characterization requires their enzymatic removal before subjecting them to mass spectrometry. Endo-β-<em>N</em>-acetylglucosaminidase H (Endo H) is one such deglycosylating enzyme that cleaves between the <em>N</em>-acetylglucosamine residue in the <em>N</em>-glycan’s di-<em>N</em>-acetylchitobiose core. Due to its commercial importance in therapeutics, we targeted a high-level <em>Streptomyces plicatus</em> Endo H expression in <em>Escherichia coli</em>. The Endo H gene was cloned under the T7 promoter containing an N-terminal 6X His tag. Shake flask expression studies in TB glucose medium resulted in 220.54 mg/L of recombinant Endo H with a specific product yield (Y<sub>P/X</sub>) of 78.07 mg/g DCW. It was purified using Ni-NTA chromatography with a recovery and purity yield of 84 % and 95 %, respectively. The specific activity of the enzyme calculated using glycoprotein RNase B as the substrate was 3.43 × 10<sup>5</sup> U/mg. It showed remarkable catalytic performance as it deglycosylated denatured RNase B even at an E:S (enzyme: substrate) ratio of 1:1000 in 1 h. Further, it deglycosylated native RNase B at an E:S ratio of 1: 10,000 with excellent efficacy. Optimization of high cell density fermentation using a fed-batch strategy resulted in a maximum Endo H production of 5.80 g/L with a Y<sub>P/X</sub> of 91.67 mg/g DCW when culture was induced at an OD<sub>600</sub> of 114.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 21-32"},"PeriodicalIF":3.7,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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
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