Enzyme and Microbial Technology最新文献_第8页

Osmoregulation by choline-based deep eutectic solvent induces electroactivity in Bacillus subtilis biofilms 胆碱深共晶溶剂的渗透调节作用诱导枯草芽孢杆菌生物膜的电活性

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-07-16 DOI: 10.1016/j.enzmictec.2024.110485

Neda Eghtesadi , Kayode Olaifa , Tri T. Pham , Vito Capriati , Obinna M. Ajunwa , Enrico Marsili

{"title":"Osmoregulation by choline-based deep eutectic solvent induces electroactivity in Bacillus subtilis biofilms","authors":"Neda Eghtesadi , Kayode Olaifa , Tri T. Pham , Vito Capriati , Obinna M. Ajunwa , Enrico Marsili","doi":"10.1016/j.enzmictec.2024.110485","DOIUrl":"10.1016/j.enzmictec.2024.110485","url":null,"abstract":"<div>Gram-positive Bacillus subtilis is a model organism for the biotechnology industry and has recently been characterized as weakly electroactive in both planktonic cultures and biofilms. Increasing the extracellular electron transfer (EET) rate in B. subtilis biofilms will help to develop an efficient microbial electrochemical technology (MET) and improve the bioproduction of high-value metabolites under electrofermentative conditions. In our previous work, we have shown that the addition of compatible solute precursors such as choline chloride (ChCl) to the growth medium formulation increases current output and biofilm formation in B. subtilis. In this work, we utilized a low-carbon tryptone yeast extract medium with added salts to further expose B. subtilis to salt stress and observe the osmoregulatory and/or nutritional effects of a D-sorbitol/choline chloride (ChCl) (1:1 mol mol−1) deep eutectic solvents (DESs) on the electroactivity of the formed biofilm. The results show that ChCl and D-sorbitol alleviate the osmotic stress induced by the addition of NaH2PO4 and KH2PO4 salts and boost biofilm production. This is probably due to the osmoprotective effect of ChCl, a precursor of the osmoprotectant glycine betaine, and the induction of electroactive exopolymeric substances within the B. subtilis biofilm. Since high ionic strength media are commonly used in microbial biotechnology, the combination of ChCl-containing DESs and salt stress could enhance biofilm-based electrofermentation processes that bring significant benefits for biotechnological applications.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110485"},"PeriodicalIF":3.4,"publicationDate":"2024-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0141022924000929/pdfft?md5=407aeace407d0e7ef745e4781151fc3c&pid=1-s2.0-S0141022924000929-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141709890","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Rational design of short-chain dehydrogenase DHDR for efficient synthesis of (S)-equol 合理设计短链脱氢酶 DHDR 以高效合成 (S)-equol

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-07-16 DOI: 10.1016/j.enzmictec.2024.110480

Weichuang Qin , Lujia Zhang , Yichen Yang , Wei Zhou , Shuting Hou , Jie Huang , Bei Gao

{"title":"Rational design of short-chain dehydrogenase DHDR for efficient synthesis of (S)-equol","authors":"Weichuang Qin , Lujia Zhang , Yichen Yang , Wei Zhou , Shuting Hou , Jie Huang , Bei Gao","doi":"10.1016/j.enzmictec.2024.110480","DOIUrl":"10.1016/j.enzmictec.2024.110480","url":null,"abstract":"<div>(S)-equol, the most influential metabolite of daidzein in vivo, has aroused great attention due to the excellent biological activities. Although existing studies have accomplished the construction of its heterologous synthetic pathway in the context of anaerobicity and inefficiency of natural strains, the low productivity of (S)-equol limits its industrial application. Here, rational design strategies based on decreasing the pocket steric hindrance and fine-tuning the pocket microenvironment to systematically redesign the binding pocket of enzyme were developed and processed to the rate-limiting enzyme dihydrodaidzein reductase in (S)-equol synthesis. After iterative combinatorial mutagenesis, an effective mutant S118G/T169A capable of significantly increasing (S)-equol yield was obtained. Computational analyses illustrated that the main reason of the increased activity relied on the decreased critical distance and more stable interacting conformation. Then, the reaction optimization was performed, and the recombinant Escherichia coli whole-cell biocatalyst harboring S118G/T169A enabled the efficient conversion of 2 mM daidzein to (S)-equol, achieving conversion rate of 84.5 %, which was 2.9 times higher than that of the parental strain expressing wide type dihydrodaidzein reductase. This study provides an effective idea and a feasible method for enzyme modification and whole-cell catalytic synthesis of (S)-equol, and will greatly accelerate the process of industrial production.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110480"},"PeriodicalIF":3.4,"publicationDate":"2024-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141697498","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

Debridement efficacy of serine protease and formulated cream by In Vitro assessment against artificial wound eschar 通过体外评估丝氨酸蛋白酶和配制膏对人工伤口焦痂的清创功效

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-07-11 DOI: 10.1016/j.enzmictec.2024.110478

Julia Yunus, Haryati Jamaluddin, Wan Rosmiza Zana Wan Dagang

{"title":"Debridement efficacy of serine protease and formulated cream by In Vitro assessment against artificial wound eschar","authors":"Julia Yunus, Haryati Jamaluddin, Wan Rosmiza Zana Wan Dagang","doi":"10.1016/j.enzmictec.2024.110478","DOIUrl":"10.1016/j.enzmictec.2024.110478","url":null,"abstract":"<div>Chronic wounds typically comprise of necrotic tissue and dried secretions, often culminating in the formation of a thick and tough layer of dead skin known as eschar. Removal of eschar is imperative to facilitate wound healing. Conventional approach for eschar removal involves surgical excision and grafting, which can be traumatic and frequently leads to viable tissue damage. There has been growing interest in the use of enzymatic agents for a gentler approach to debridement, utilizing proteolytic enzymes. In this study, a purified intracellular recombinant serine protease from Bacillus sp. (SPB) and its cream formulation were employed to evaluate their ability to degrade artificial wound eschar; composed of collagen, fibrin, and elastin. Degradation was assessed based on percentage weight reduction of eschar biomass, analysis via sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), and scanning electron microscopy (SEM). Both SPB and its cream formulation were able to degrade up to 50 % artificial wound eschar, with the SPB cream maintaining its degradation efficiency for up to 24 hours. Additionally, the SPB-based cream demonstrated the ability to hydrolyze proteinaceous components of eschars individually (fibrin and collagen) as determined through qualitative assessment. These findings suggest that SPB holds promise for the debridement of wound eschar.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110478"},"PeriodicalIF":3.4,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141695010","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

Control of Staphylococcus epidermidis biofilm by surfactins of an endophytic bacterium Bacillus sp. 15 F 内生细菌芽孢杆菌的表面活性剂对表皮葡萄球菌生物膜的控制 15 F

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-07-03 DOI: 10.1016/j.enzmictec.2024.110477

Marwa Jardak , Raphaël Lami , Oumaima Saadaoui , Hajer Jlidi , Didier Stien , Sami Aifa , Sami Mnif

{"title":"Control of Staphylococcus epidermidis biofilm by surfactins of an endophytic bacterium Bacillus sp. 15 F","authors":"Marwa Jardak , Raphaël Lami , Oumaima Saadaoui , Hajer Jlidi , Didier Stien , Sami Aifa , Sami Mnif","doi":"10.1016/j.enzmictec.2024.110477","DOIUrl":"https://doi.org/10.1016/j.enzmictec.2024.110477","url":null,"abstract":"<div>The present paper deals with the preparation and annotation of a surfactin(s) derived from a culture of the endophytic bacterium Bacillus 15 F. The LC-MS analysis of the acetonitrile fraction confirmed the presence of surfactins Leu/Ile7 C15, Leu/Ile7 C14 and Leu/Ile7 C13 with [M+H]+ at m/z 1036.6895, 1022.6741 and 1008.6581, respectively. Various concentrations of the surfactin(s) (hereafter referred to as surfactin-15 F) were used to reduce the adhesion of Staphylococcus epidermidis S61, which served as a model for studying antibiofilm activity on polystyrene surfaces. Incubation of Staphylococcus epidermidis S61 with 62.5 µg/ml of surfactin-15 F resulted in almost complete inhibition of biofilm formation (90.3 ± 3.33 %), and a significant reduction of cell viability (resazurin-based fluorescence was more than 200 times lower). The antiadhesive effect of surfactin-15 F was confirmed by scanning electron microscopy. Surfactin-15 F demonstrated an eradication effect against preformed biofilm, causing severe disruption of Staphylococcus epidermidis S61 biofilm structure and reducing viability. The results suggest that surfactins produced by endophytic bacteria could be an alternative to synthetic products. Surfactin-15 F, used in wound dressings, demonstrated an efficient treatment of the preformed Staphylococcus epidermidis S61 biofilm, and thus having a great potential in medical applications.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110477"},"PeriodicalIF":3.4,"publicationDate":"2024-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141607715","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

Identification of an endonuclease and N6-adenine methyltransferase from Ureaplasma parvum SV3F4 strain 鉴定副脲原体 SV3F4 株的内切酶和 N6-腺嘌呤甲基转移酶。

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-26 DOI: 10.1016/j.enzmictec.2024.110471

Heng Ning Wu , Yuya Fujisawa , Zenzaburo Tozuka , Alexey Fomenkov , Yukiko Nakura , Shin-ichiro Kajiyama , Shinsuke Fujiwara , Kiyoshi Yasukawa , Richard J. Roberts , Itaru Yanagihara

{"title":"Identification of an endonuclease and N6-adenine methyltransferase from Ureaplasma parvum SV3F4 strain","authors":"Heng Ning Wu , Yuya Fujisawa , Zenzaburo Tozuka , Alexey Fomenkov , Yukiko Nakura , Shin-ichiro Kajiyama , Shinsuke Fujiwara , Kiyoshi Yasukawa , Richard J. Roberts , Itaru Yanagihara","doi":"10.1016/j.enzmictec.2024.110471","DOIUrl":"10.1016/j.enzmictec.2024.110471","url":null,"abstract":"<div>Here, we report a novel endonuclease and N6-adenine DNA methyltransferase (m6A methyltransferase) in the Ureaplasma parvum SV3F4 strain. Our previous study found that the SV3F4 strain carries 17 unique genes, which are not encoded in the two previously reported U. parvum serovar 3 strain, OMC-P162 and ATCC 700970. Of these 17 unique genes, UP3_c0261 and UP3_c0262, were originally annotated as encoding hypothetical proteins. Comparative genomics analyses more recently indicated they encode a Type II restriction endonuclease and an m6A methyltransferase, respectively. The UP3_c0261 and UP3_c0262 genes were individually expressed and purified in Escherichia coli. The UP3_c0261 recombinant protein showed endonuclease activity on the pT7Blue vector, recognizing and cleaving a GTNAC motif, resulting in a 5 base 5’ extension. The UP3_c0261 protein digested a polymerase chain reaction (PCR) product harboring the GTNAC motif. The endonuclease UP3_c0261 was designated as UpaF4I. Treatment of the PCR product with the recombinant protein UP3_c0262 completely blocked the restriction enzyme activity of UpaF4I. Analysis of the treated PCR product harboring a modified nucleotide by UP3_c0262 with HPLC-MS/MS and MS/MS showed that UP3_c0262 was an m6A methyltransferase containing a methylated A residue in both DNA strands of the GTNAC motif. Whole genome methylation analysis of SV3F4 showed that 99.9 % of the GTNAC motif was m6A modified. These results suggest the UP3_c0261 and UP3_c0262 genes may act as a novel Type II restriction-modification system in the Ureaplasma SV3F4 strain.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110471"},"PeriodicalIF":3.4,"publicationDate":"2024-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0141022924000784/pdfft?md5=99c87b539386921e1e06916b966ff332&pid=1-s2.0-S0141022924000784-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141497491","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Tailored expression of ICCM cutinase in engineered Escherichia coli for efficient polyethylene terephthalate hydrolysis 在工程大肠杆菌中定制表达 ICCM cutinase，以实现聚对苯二甲酸乙二醇酯的高效水解。

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-26 DOI: 10.1016/j.enzmictec.2024.110476

Hsing-Ning Ma, Chuan-Chieh Hsiang, I-Son Ng

{"title":"Tailored expression of ICCM cutinase in engineered Escherichia coli for efficient polyethylene terephthalate hydrolysis","authors":"Hsing-Ning Ma, Chuan-Chieh Hsiang, I-Son Ng","doi":"10.1016/j.enzmictec.2024.110476","DOIUrl":"10.1016/j.enzmictec.2024.110476","url":null,"abstract":"<div>Enzymatic depolymerization of PET waste emerges as a crucial and sustainable solution for combating environmental pollution. Over the past decade, PET hydrolytic enzymes, such as PETase from Ideonella sakaiensis (IsPETases), leaf compost cutinases (LCC), and lipases, have been subjected to rational mutation to enhance their enzymatic properties. ICCM, one of the best LCC mutants, was selected for overexpression in Escherichia coli BL21(DE3) for in vitro PET degradation. However, overexpressing ICCM presents challenges due to its low productivity. A new stress-inducible T7RNA polymerase-regulating E. coli strain, ASIAhsp, which significantly enhances ICCM production by 72.8 % and achieves higher enzyme solubility than other strains. The optimal cultural condition at 30 °C with high agitation, corresponding to high dissolved oxygen levels, has brought the maximum productivity of ICCM and high PET-hydrolytic activity. The most effective PET biodegradation using crude or pure ICCM occurred at pH 10 and 60 °C. Moreover, ICCM exhibited remarkable thermostability, retaining 60 % activity after a 5-day reaction at 60 °C. Notably, crude ICCM eliminates the need for purification and efficiently degrades PET films.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"179 ","pages":"Article 110476"},"PeriodicalIF":3.4,"publicationDate":"2024-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141466986","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

Development of a bioluminescent homogenous nanobody-based immunoassay for the detection of prostate-specific antigen (PSA) 开发基于生物发光均质纳米抗体的免疫测定法，用于检测前列腺特异性抗原（PSA）。

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-25 DOI: 10.1016/j.enzmictec.2024.110474

Mahmoud Esraa Baghdadi , Rahman Emamzadeh , Mahboobeh Nazari , Elisa Michelini

{"title":"Development of a bioluminescent homogenous nanobody-based immunoassay for the detection of prostate-specific antigen (PSA)","authors":"Mahmoud Esraa Baghdadi , Rahman Emamzadeh , Mahboobeh Nazari , Elisa Michelini","doi":"10.1016/j.enzmictec.2024.110474","DOIUrl":"10.1016/j.enzmictec.2024.110474","url":null,"abstract":"<div>Prostate cancer is the most prevalent cancer in men. At present, the diagnosis and screening of prostate cancer rely on the essential biomarker known as prostate-specific antigen (PSA). The main purpose of this study was to develop a novel immunoassay for the detection of PSA based on a tri-part split-nanoluciferase system and a nanobody targeting PSA. In our approach, two small components of the split-nanoluciferase, referred to as β9 and β10, were individually fused to two anti-PSA nanobodies, N7 and N23. When these proteins bind to PSA and in the presence of the third nanoluciferase component, called Δ11S, the split-nanoluciferase components are brought into close proximity, facilitating the reassembly of the active nanoluciferase and activation of luminescence. These proteins were expressed in a bacterial expression system, purified, and employed for the intended immunoassay. The developed immunoassay demonstrated the capability to sensitively detect PSA within a linear range from 1.0 to 20.0 ng/mL with LOD of 0.4 ng/mL, and the results obtained through this immunoassay agreed with those derived from the ELISA. Our study indicates that the homogeneous immunoassay developed with nanobodies exhibits remarkable specificity for PSA and can serve as a reliable, fast, and user-friendly test for detecting PSA.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"180 ","pages":"Article 110474"},"PeriodicalIF":3.4,"publicationDate":"2024-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141466987","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

Biotransformation of ferulic acid into vanillyl alcohol and vanillic acid employing thermophilic bacterium Caldimonas thermodepolymerans 利用嗜热细菌 Caldimonas thermodepolymerans 将阿魏酸生物转化为香草醇和香草酸。

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-23 DOI: 10.1016/j.enzmictec.2024.110475

Vendula Hrabalová , Tomáš Opial , Jana Musilová , Karel Sedlář , Stanislav Obruča

{"title":"Biotransformation of ferulic acid into vanillyl alcohol and vanillic acid employing thermophilic bacterium Caldimonas thermodepolymerans","authors":"Vendula Hrabalová , Tomáš Opial , Jana Musilová , Karel Sedlář , Stanislav Obruča","doi":"10.1016/j.enzmictec.2024.110475","DOIUrl":"10.1016/j.enzmictec.2024.110475","url":null,"abstract":"<div>Caldimonas thermodepolymerans, a Gram-negative, moderately thermophilic bacterium, exhibits a remarkable biotechnological potential. Given the presence of genes in its genome dedicated to the metabolization of ferulic acid (FA), this study aimed to explore the bacterium's capability for biotransforming FA into high-value metabolites. The results unequivocally demonstrate the bacterium's proficiency in the efficient and rapid conversion of FA into vanillyl alcohol (VOH) and vanillic acid (VA). By manipulating key cultivation parameters, such as adjusting initial FA doses and varying cultivation periods, the product profile can be tailored. Higher initial doses and shorter cultivation periods favor the production of VOH, while lower FA doses and extended cultivation periods lead to the predominant formation of VA. Furthermore, the process can be operated in a repeated-batch scenario. This underscores the potential of C. thermodepolymerans for industrial biotransformation of FA, presenting a promising avenue for leveraging its capabilities in practical applications.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"179 ","pages":"Article 110475"},"PeriodicalIF":3.4,"publicationDate":"2024-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141456000","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

Advances in the understanding of the production, modification and applications of xylanases in the food industry 进一步了解木聚糖酶的生产、改性和在食品工业中的应用。

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-17 DOI: 10.1016/j.enzmictec.2024.110473

Dongdong Mu , Penglong Li , Tiange Ma , Dehua Wei , Manuel Montalbán-López , Yaqian Ai , Xuefeng Wu , Yifeng Wang , Xu Li , Xingjiang Li

{"title":"Advances in the understanding of the production, modification and applications of xylanases in the food industry","authors":"Dongdong Mu , Penglong Li , Tiange Ma , Dehua Wei , Manuel Montalbán-López , Yaqian Ai , Xuefeng Wu , Yifeng Wang , Xu Li , Xingjiang Li","doi":"10.1016/j.enzmictec.2024.110473","DOIUrl":"10.1016/j.enzmictec.2024.110473","url":null,"abstract":"<div>Xylanases have broad applications in the food industry to decompose the complex carbohydrate xylan. This is applicable to enhance juice clarity, improve dough softness, or reduce beer turbidity. It can also be used to produce prebiotics and increase the nutritional value in foodstuff. However, the low yield and poor stability of most natural xylanases hinders their further applications. Therefore, it is imperative to explore higher-quality xylanases to address the potential challenges that appear in the food industry and to comprehensively improve the production, modification, and utilization of xylanases. Xylanases, due to their various sources, exhibit diverse characteristics that affect production and activity. Most fungi are suitable for solid-state fermentation to produce xylanases, but in liquid fermentation, microbial metabolism is more vigorous, resulting in higher yield. Fungi produce higher xylanase activity, but bacterial xylanases perform better than fungal ones under certain extreme conditions (high temperature, extreme pH). Gene and protein engineering technology helps to improve the production efficiency of xylanases and enhances their thermal stability and catalytic properties.</div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"179 ","pages":"Article 110473"},"PeriodicalIF":3.4,"publicationDate":"2024-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141450142","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

Production of lactulose from lactose using a novel cellobiose 2-epimerase from Clostridium disporicum 利用一种来自双孔梭状芽孢杆菌的新型纤维生物糖 2-epimerase 从乳糖中生产乳纤维素

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2024-06-14 DOI: 10.1016/j.enzmictec.2024.110466

Bohua Wang , Song Lei , Qingqin Li , Yushuang Luo

引用次数: 0