Process Biochemistry最新文献_第6页

Optimized nitrogen removal in low-carbon settings via sequencing batch reactors with vermiculite-enveloped layered double hydroxides bio-fillers

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-19 DOI: 10.1016/j.procbio.2025.01.016

Lv Xi, Zhang Peng, Zhang Qiwu, He Xiaoman

引用次数: 0

Improving eicosapentaenoic acid yield by constructing an enzyme-constrained model of Schizochytrium

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-17 DOI: 10.1016/j.procbio.2025.01.010

Zijian Hu , Dechun Kong , Tianjun Gan , Yuhong Xin , Yuetong Wang , Tianqiong Shi , Chao Ye

{"title":"Improving eicosapentaenoic acid yield by constructing an enzyme-constrained model of Schizochytrium","authors":"Zijian Hu , Dechun Kong , Tianjun Gan , Yuhong Xin , Yuetong Wang , Tianqiong Shi , Chao Ye","doi":"10.1016/j.procbio.2025.01.010","DOIUrl":"10.1016/j.procbio.2025.01.010","url":null,"abstract":"<div><div>Eicosapentaenoic acid (EPA), an essential omega-3 polyunsaturated fatty acid (PUFA), cannot be produced by the human body. It finds applications in various fields, including health foods, pharmaceuticals, and animal feed. <em>Schizochytrium</em> sp., an oleaginous microorganism rich in PUFAs, holds promise for EPA production. However, its complex metabolic network limits its full potential. To address this challenge, we constructed a detailed enzyme-constrained model eciCY1170_DHA of <em>Schizochytrium</em>'s metabolism. This model incorporated 1083 genes, 5236 reactions, and 2989 metabolites. We then used this model to simulate fermentation conditions and validated our predictions through experiments. Our research results indicate that the optimal nitrogen source absorption rate is 0.7692 mmol/gDW/h, and the optimal oxygen absorption rate is 3.41 mmol/gDW/h. When both absorption rates are higher or lower than the optimal values, they will hinder EPA production. Conclusions drawn from simulations and experiments show that by adjusting the nitrogen source concentration, Ventilation volume, and agitation speed, the maximum yield of EPA reached 1.09 g/L in a 5 L fermenter. By analyzing protein requirements, we identified 20 potential targets predicted to enhance EPA production. This study provides new ideas for the optimization of medium composition and strain modification for the industrial production of EPA using <em>Schizochytrium</em>.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 238-247"},"PeriodicalIF":3.7,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099622","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

De novo carbon monoxide dehydrogenase and carbonic anhydrase using molecular dynamics and deep generative model

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-16 DOI: 10.1016/j.procbio.2025.01.013

Ruei-En Hu , Chang-Chun Chang , Tzu-Hao Chen , Ching-Ping Chang , Chi-Hua Yu , I-Son Ng

{"title":"De novo carbon monoxide dehydrogenase and carbonic anhydrase using molecular dynamics and deep generative model","authors":"Ruei-En Hu , Chang-Chun Chang , Tzu-Hao Chen , Ching-Ping Chang , Chi-Hua Yu , I-Son Ng","doi":"10.1016/j.procbio.2025.01.013","DOIUrl":"10.1016/j.procbio.2025.01.013","url":null,"abstract":"<div><div>Carbon monoxide dehydrogenase (CODH) and carbonic anhydrase (CA) play crucial roles in cellular metabolism by catalyzing the interconversion of carbon monoxide, carbon dioxide, and bicarbonate. However, the diversity of both enzymes remains unclear. This study integrates deep generative models and molecular dynamics simulations to streamline the design of novel CODH and CA variants. Using highly active enzymes from <em>Carboxydothermus hydrogenoformans</em> (PDB: 1SU8) and human carbonic anhydrase II (PDB:1HEB) as templates, we engineered <em>de novo</em> protein structures with enzymatic activities. Deep generative models including RFdiffusion, ProteinMPNN, CLEAN, and AlphaFold3 were employed to design novel CODH variants. Among all candidates, CODH2206 showed superior stability and activity in simulations but protein expressed as inclusion bodies in <em>E. coli</em> BL21(DE3) and improved in C43(DE3). Further characterization revealed that CODH2206 exhibited higher activity at pH 8. To resolve the quality and quantity of <em>de novo</em> enzymes, we applied SoDoPe solubility and trRosetta structure prediction for pixel-to-protein creation. Finally, hCAd3 activity increased 5-folds when chaperones and rare codons were involved in the system. This pipeline has high potential to generate diverse enzymes, advancing protein engineering for the creation of biocatalysts in the future.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 221-228"},"PeriodicalIF":3.7,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094484","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

The impact of low COD/N ratio on denitrification performance and microbial community in an intermittent aeration moving bed membrane bioreactor

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-15 DOI: 10.1016/j.procbio.2025.01.012

Jinmao Ye , Lin Huang , Yu Zhang , Changming Zhong

{"title":"The impact of low COD/N ratio on denitrification performance and microbial community in an intermittent aeration moving bed membrane bioreactor","authors":"Jinmao Ye , Lin Huang , Yu Zhang , Changming Zhong","doi":"10.1016/j.procbio.2025.01.012","DOIUrl":"10.1016/j.procbio.2025.01.012","url":null,"abstract":"<div><div>Conventional biological nutrient removal (BNR) processes for treating wastewater from ionic rare earth mining areas with low COD/N ratios typically require a significant supply of organic carbon sources. To overcome this limitation, an intermittently aerated moving bed membrane bioreactor (MBMBR) was utilized to facilitate simultaneous partial nitrification and denitrification (SPND) under low COD/N conditions. At a mixing-to-aeration duration of 30 min:20 min, and a COD/N ratio of 3.5, removal rates of 99.88 % for NH<sub>4</sub><sup>+</sup>-N, 86.14 % for TN, and 91.62 % for COD were achieved. 16S rRNA sequencing revealed a significant impact of COD/N ratio on the microbial community structure. Notably, at a COD/N ratio of 3.5, <em>SM1A02</em>, known for its nitrification and anaerobic ammonium oxidation capabilities, was identified with a relative abundance of 10.32 %. With the further reduction of the COD/N ratio, the abundance of <em>SM1A02</em> showed a progressive decline. Fluorescence analysis of extracellular polymeric substances (EPS) from both the mixed liquor and membrane surface sludge revealed that proteins and humic acids were the predominant components of EPS, with proteins identified as the primary contributors to membrane fouling. Meanwhile, a reduction in the COD concentration was found to mitigate membrane fouling. This study offers key strategies for minimizing energy consumption and controlling membrane fouling during the treatment of low COD/N ratio wastewater through the application of MBMBR technology.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 189-201"},"PeriodicalIF":3.7,"publicationDate":"2025-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099605","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

Proteome analysis of the spontaneous oscillatory behavior in 1,3-propanediol production from glycerol by Clostridium butyricum

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-13 DOI: 10.1016/j.procbio.2025.01.011

Jin-Dong Han, Ling-Yun Liang, Pu-Yang Liang, Xiao-Li Wang, Ya-Qin Sun, Zhi-Long Xiu

{"title":"Proteome analysis of the spontaneous oscillatory behavior in 1,3-propanediol production from glycerol by Clostridium butyricum","authors":"Jin-Dong Han, Ling-Yun Liang, Pu-Yang Liang, Xiao-Li Wang, Ya-Qin Sun, Zhi-Long Xiu","doi":"10.1016/j.procbio.2025.01.011","DOIUrl":"10.1016/j.procbio.2025.01.011","url":null,"abstract":"<div><div>The oscillatory cultures in biological systems offer an opportunity for understanding the metabolic mechanism, regulation, and constraint. This study focuses on the particular spontaneous oscillation during continuous 1,3-propanediol (1,3-PDO) fermentation by <em>Clostridium butyricum</em>. A sustained oscillation occurred was triggered by 88 g/L glycerol at a dilution rate of 0.048 h<sup>−1</sup>. The oscillatory behavior started at approximately 35 h and sustained for over 530 h with an average oscillation period of 35 h. Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis indicated that a total of 46 proteins associated with glycerol metabolism were characterized. Aldehyde-alcohol dehydrogenase (AdhE), pyruvate:ferredoxin (lavodoxin) oxidoreductase (PFOR), and L-lactate dehydrogenase (LDH) with high centrality degree and compact coefficient were identified as the most crucial proteins in the protein-protein interaction network. Various proteins involved in Fe<sup>2+</sup> regulation, such as AdhE, PFOR, glycerol dehydrogenase, 1,3-propanediol oxydoreductase, glycerol dehydratase activating protein, pyruvate formate lyase, nitrogenase, ferredoxin:NADP<sup>+</sup> reductase, and hydrogenase were crucial for the spontaneous oscillation. These findings demonstrate that the level of Fe<sup>2+</sup> influences the coordination of spontaneous oscillation in glycerol conversion to 1,3-PDO in <em>C. butyricum</em>. Finally, a sustained oscillatory behavior induced in response to a change in Fe<sup>2+</sup> concentration further verifies Fe<sup>2+</sup> limitation as a valve to generate oscillation<em>.</em></div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 180-188"},"PeriodicalIF":3.7,"publicationDate":"2025-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099623","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

The bifunctional enzymatic catalysis of maize waste for simultaneous production of arabinose and xylose

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-11 DOI: 10.1016/j.procbio.2025.01.008

Jia Chen , Mei Li , Lulu Cao , Hao Chen , Jung-Kul Lee , Vipin Chandra Kalia , Chunjie Gong

{"title":"The bifunctional enzymatic catalysis of maize waste for simultaneous production of arabinose and xylose","authors":"Jia Chen , Mei Li , Lulu Cao , Hao Chen , Jung-Kul Lee , Vipin Chandra Kalia , Chunjie Gong","doi":"10.1016/j.procbio.2025.01.008","DOIUrl":"10.1016/j.procbio.2025.01.008","url":null,"abstract":"<div><div>With the increase in environmental pollution, bio-manufacturing is gaining more attention. Plant sugars, including xylose and arabinose, could be utilized to produce bio-based chemicals. This study detected a putative gene encoding bifunctional xylosidase/arabinosidase in soil metagenome and isolated a bacterium, <em>Sphingobacterium</em>. The putative gene was expressed exogenously in <em>Escherichia coli</em> BL21 (DE3), and a bifunctional enzyme of approximately 35.9 kDa was obtained. The purified enzyme exhibited xylosidase and arabinosidase activities against p-nitrophenol-β-D-xyloside and p-nitrophenol-α-L-arabinofuranoside. The optimum temperature for both enzymatic activities was 60 °C, whereas the pH optima for xylosidase and arabinosidase were 7.0 and 8.0, respectively. Using the bifunctional enzyme catalysis, 1.35 mg of xylose was obtained from 20 mg of maize stalk. Meanwhile, 2.238 mg of arabinose was obtained from 20 mg of maize cob. Two sugars co-production from biomass waste using the bifunctional xylosidase/arabinosidase showed promising applications in practice.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 161-167"},"PeriodicalIF":3.7,"publicationDate":"2025-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094477","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

Synthesis of structured lipids using microalgae oil and capric acid via a two-step enzyme reaction

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-10 DOI: 10.1016/j.procbio.2025.01.009

Yu Jin Lee , Heon-Woong Kim , Junsoo Lee , Byung Hee Kim , In-Hwan Kim

{"title":"Synthesis of structured lipids using microalgae oil and capric acid via a two-step enzyme reaction","authors":"Yu Jin Lee , Heon-Woong Kim , Junsoo Lee , Byung Hee Kim , In-Hwan Kim","doi":"10.1016/j.procbio.2025.01.009","DOIUrl":"10.1016/j.procbio.2025.01.009","url":null,"abstract":"<div><div><em>n</em>-3 Docosahexaenoic acid (<em>n</em>-3 DHA) and <em>n</em>-6 docosapentaenoic acid (<em>n</em>-6 DPA) are contained abundantly in microalgae oil. The present study aimed to synthesize structured triacylglycerol (TAG) with <em>n</em>-3 DHA, <em>n</em>-6 DPA, and capric acid via a two-step lipase-catalyzed reaction. Microalgae oil and capric acid were used as substrates to synthesize structured TAG. In the first step, <em>n</em>-3 DHA and <em>n</em>-6 DPA were effectively enriched from an initial value of approximately 53–86 mol% in the glycerides of the microalgae oil obtained via Lipozyme RM IM-catalyzed ethanolysis. The optimum conditions for ethanolysis were a temperature of 25 °C, an enzyme loading of 15 %, and a molar ratio of 1:1 (fatty acid in microalgae oil to ethanol). In the second step, capric acid was incorporated into the hydroxyl group of glycerides obtained through ethanolysis to synthesize structured TAG using two different lipases. The effects of temperature and vacuum on TAG conversion were investigated to optimize lipase-catalyzed esterification. For both lipases, the optimum conditions were a temperature of 60 °C and a vacuum of 5 mmHg. Maximum TAG conversion was achieved with Lipozyme 435, whereas Lipozyme RM IM exhibited higher regiospecificity toward the <em>sn</em>-1,3 positions of TAG.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 213-220"},"PeriodicalIF":3.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094482","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

Synergizing food waste management and microalgae biorefinery for bioenergy production: Recent advance on direct and indirect conversion pathways

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-10 DOI: 10.1016/j.procbio.2025.01.006

Adityas Agung Ramandani , Sze Ying Lee , Anet Režek Jambrak , Wei-Hsin Chen , Jun Wei Lim , Kuan Shiong Khoo

{"title":"Synergizing food waste management and microalgae biorefinery for bioenergy production: Recent advance on direct and indirect conversion pathways","authors":"Adityas Agung Ramandani , Sze Ying Lee , Anet Režek Jambrak , Wei-Hsin Chen , Jun Wei Lim , Kuan Shiong Khoo","doi":"10.1016/j.procbio.2025.01.006","DOIUrl":"10.1016/j.procbio.2025.01.006","url":null,"abstract":"<div><div>Food waste is a persistent global environmental issue that contributes to global warming and climate change by releasing significant amounts of greenhouse gases as it decomposes in landfills. Converting food waste into bioenergy could serve as a sustainable solution. Direct conversion of food waste through methods like anaerobic digestion, fermentation, and pyrolysis, produces diverse energy products. Besides, the indirect approach of cultivating microalgae using food waste as alternative medium provides a sustainable solution, as microalgae can assimilate nutrient-rich components (e.g., nitrogen, phosphorus, and carbon), converting them into valuable biomass that can be processed into biofuels. This review work provides a holistic review of food waste-to-energy conversion methods, both direct and indirect, evaluating their feasibility and benefits. Specifically, a comprehensive analysis of using microalgae grown on food waste for biofuel production is provided, offering insights into how the method could effectively address both environmental and energy crises, and contribute to sustainable development goals. Future research should focus on enhancing conversion process efficiency, optimizing microalgae bioprocess, and scaling-up these technologies to industrial levels, while addressing challenges such as economic feasibility, supportive policies, and robust supply chains. Collaboration among industry, academia, and government is essential to boost the global implementation of these technologies.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"151 ","pages":"Pages 14-26"},"PeriodicalIF":3.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143140379","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

Substrate bio-imprinted CLEAs of type B feruloyl esterase from Aspergillus terreus: A selective heterogeneous biocatalyst towards butyl caffeate

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-10 DOI: 10.1016/j.procbio.2025.01.004

Daniel A. Grajales-Hernández , Mariana A. Armendáriz-Ruiz , Jorge A. Rodríguez , Susana Velasco-Lozano , Fernando López-Gallego , Juan Carlos Mateos-Díaz

{"title":"Substrate bio-imprinted CLEAs of type B feruloyl esterase from Aspergillus terreus: A selective heterogeneous biocatalyst towards butyl caffeate","authors":"Daniel A. Grajales-Hernández , Mariana A. Armendáriz-Ruiz , Jorge A. Rodríguez , Susana Velasco-Lozano , Fernando López-Gallego , Juan Carlos Mateos-Díaz","doi":"10.1016/j.procbio.2025.01.004","DOIUrl":"10.1016/j.procbio.2025.01.004","url":null,"abstract":"<div><div>The biological properties of caffeic acid esters, compel the search for selective biocatalysts for its synthesis since caffeic acid is generally mixed with ferulic acid in nature. Here, we employed a type B feruloyl esterase from <em>Aspergillus terreus</em> bio-imprinted and crosslinked (AtFAEB-CLEAs) to increase its selectivity towards the synthesis of butyl caffeate in caffeic/ferulic acid equimolar mixtures. The best AtFAEB-CLEAs were prepared using n-butanol/caffeic acid (50 mM) mixture for enzyme precipitation/bio-imprinting, polyethyleneimine as co-feeder, and glutaraldehyde as a crosslinker. Selected AtFAEB-CLEAs showed an expressed activity 2.6-fold higher (218 U·mg<sup>−1</sup>) than free enzyme, and a 13.5-fold enhancement in synthesis selectivity on a hexane: n-butanol: water system, inverting the initial preference for ferulic acid towards caffeic acid. Intrinsic protein fluorescence profiles strongly suggest a <em>freeze-up</em> of conformational changes induced by bioimprinting in the AtFAEB. Additionally, immobilization increased the thermal and solvent stability of AtFAEB-CLEAS 7.9 and 5.7-fold, respectively. Final reaction tests (0.1 mg/mL) achieved 88 % conversion in 6 hours and demonstrated a strong preference for butyl caffeate synthesis of 26-fold in the first hour of reaction. Improvement through CLEA fabrication of selectivity and stability of AtFAEB could potentially lead to the valorization of agro-industrial by-products into relevant molecules for the cosmetic and pharmaceutic industries.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 168-179"},"PeriodicalIF":3.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094481","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 bacterial chitosanase production using soybean meal hydrolysate: Insights into biochemical and hydrolysis characteristics

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-10 DOI: 10.1016/j.procbio.2025.01.007

Oanh Thi Kim Nguyen , Po-Ting Chen , Parushi Nargotra , Sheng-Chia Chen , Chih-Yu Cheng , Hui-Min David Wang , Yung-Chuan Liu , Chia-Hung Kuo

{"title":"Sustainable bacterial chitosanase production using soybean meal hydrolysate: Insights into biochemical and hydrolysis characteristics","authors":"Oanh Thi Kim Nguyen , Po-Ting Chen , Parushi Nargotra , Sheng-Chia Chen , Chih-Yu Cheng , Hui-Min David Wang , Yung-Chuan Liu , Chia-Hung Kuo","doi":"10.1016/j.procbio.2025.01.007","DOIUrl":"10.1016/j.procbio.2025.01.007","url":null,"abstract":"<div><div>The chitosanase Csn from <em>Bacillus subtilis</em> 168, previously recombinantly expressed in <em>B. subtilis</em> PT5 called PT5(MT1-Csn) had demonstrated potential for converting chitosan into chitosan-oligosaccharides (COS). Herein, a new fermentation medium containing soybean meal hydrolysate (SMH), an oil byproduct, was used for enhancing PT5(MT1-Csn) chitosanase activity. The purified PT5(MT1-Csn) exhibited activity (1018.58 U mL<sup>−1</sup>) 11.5 times higher than the wild-type (WT) enzyme at pH 5.0 and 50 °C. Both PT5(MT1-Csn) and WT exhibited similar pH stability (3.0–9.0) and thermostability. The melting temperature (<em>Tm</em>) values of PT5(MT1-Csn) (51.38 °C ± 0.11) and WT (51.68 °C ± 0.03) were similar. After hydrolysis, chitosan-oligosaccharides (COS) without glucosamine or acetylglucosamine were produced, with a degree of polymerization between 2 and 4. The findings of the current study suggest that SMH can be effectively utilized to not only enhance the PT5(MT1-Csn) activity and reduce enzyme production cost but also to effectively valorize the oil byproducts.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 202-212"},"PeriodicalIF":3.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094483","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