Protein expression and purification最新文献_第9页

Characterization of recombinant phytase of Klebsiella sp. and the influence of novel 3-phytase on mineral solubility in broiler diets under an in vitro digestion assay 克雷伯氏菌重组植酸酶的特性以及新型 3-植酸酶在体外消化试验中对肉鸡日粮中矿物质溶解度的影响

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-27 DOI: 10.1016/j.pep.2024.106489

Mohammad Houshyar , Ali Asghar Saki , Mohammad Yousef Alikhani , Michael Richard Bedford , Meysam Soleimani , Farideh Kamarehei

{"title":"Characterization of recombinant phytase of Klebsiella sp. and the influence of novel 3-phytase on mineral solubility in broiler diets under an in vitro digestion assay","authors":"Mohammad Houshyar , Ali Asghar Saki , Mohammad Yousef Alikhani , Michael Richard Bedford , Meysam Soleimani , Farideh Kamarehei","doi":"10.1016/j.pep.2024.106489","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106489","url":null,"abstract":"<div><p>Phytate (inositol hexaphosphate) is the major storage form of phosphorus (P) in nature, and phytases catalyze the hydrolysis of P from phytate and the formation of inositol phosphate isomers. In this study, a bacterium that produces phytase was isolated in a phytase screening medium. The bacterium was identified as <em>Klebsiella sp.</em> using phenotypic and molecular techniques. The <em>PhyK</em> phytase gene was successfully amplified from the genome, inserted into the pET-21a (+) vector, and expressed as a recombinant protein in <em>E. Coli BL21</em>. The efficiency of a laboratory phytase (Lab-Ph<em>, PhyK</em> phytase) was determined and compared with a commercial phytase (Com-Ph, Quantum Blue 40P phytase, AB Vista) under an in vitro digestion assay. The native signal peptide effectively facilitated the translocation of the protein to the periplasmic space of <em>E. Coli BL21</em>, resulting in the proper folding of the protein and the manifestation of desirable enzyme activity. The Lab-Ph displayed the temperature and pH optima at 50 °C and 5 respectively. In addition, the Lab-Ph was inactivated at 80 °C. Under an in vitro digestion assay condition, Lab-Ph improved the P solubility coefficient in broiler diets. In comparison, the Com-Ph significantly increased the P solubility coefficient even when compared with the Lab-Ph. In summary, this study has shown that Lab-Ph possesses the necessary biochemical properties to be used in various industrial applications. However, Lab-Ph is extremely sensitive to heat treatment. The Lab-Ph and Com-Ph under an in vitro digestion assay improved the solubility coefficient of P in the broiler diet.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"220 ","pages":"Article 106489"},"PeriodicalIF":1.6,"publicationDate":"2024-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140842966","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Unexpected tobacco etch virus (TEV) protease cleavage of recombinant human proteins 烟草蚀刻病毒（TEV）蛋白酶意外裂解重组人类蛋白质

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-26 DOI: 10.1016/j.pep.2024.106488

Lauren P. Beaumont, Jennifer Mehalko, Adam Johnson, Vanessa E. Wall, Dominic Esposito

引用次数: 0

Expression, purification and preliminary crystallographic analysis of bacterial transmembrane protein EfeU for iron import 用于铁输入的细菌跨膜蛋白 EfeU 的表达、纯化和初步结晶分析。

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-23 DOI: 10.1016/j.pep.2024.106487

Kenji Okumura , Bunzo Mikami , Sayoko Oiki , Kohei Ogura , Wataru Hashimoto

引用次数: 0

Expression and biochemical characterization of a novel thermostable alkaline β-1,3–1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1 来自嗜碱性芽孢杆菌 G1 的新型恒温碱性 β-1,3-1,4-葡聚糖酶（地衣酶）的表达和生化特性鉴定

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-19 DOI: 10.1016/j.pep.2024.106486

Noor Liana Mat Yajit , Noor Haza Fazlin Hashim , Rosli Mohd Illias , Abdul Munir Abdul Murad

{"title":"Expression and biochemical characterization of a novel thermostable alkaline β-1,3–1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1","authors":"Noor Liana Mat Yajit , Noor Haza Fazlin Hashim , Rosli Mohd Illias , Abdul Munir Abdul Murad","doi":"10.1016/j.pep.2024.106486","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106486","url":null,"abstract":"<div><p>New thermostable β-1,3–1,4-glucanase (lichenase) designated as Blg29 was expressed and purified from a locally isolated alkaliphilic bacteria <em>Bacillus lehensis</em> G1. The genome sequence of <em>B. lehensis</em> predicted an open reading frame of Blg29 with a deduced of 249 amino acids and a molecular weight of 28.99 kDa. The gene encoding for <em>Blg29</em> was successfully amplified via PCR and subsequently expressed as a recombinant protein using the <em>E. coli</em> expression system. Recombinant Blg29 was produced as a soluble form and further purified via immobilized metal ion affinity chromatography (IMAC). Based on biochemical characterization, recombinant Blg29 showed optimal activity at pH9 and temperature 60 °C respectively. This enzyme was stable for more than 2 h, incubated at 50 °C, and could withstand ∼50 % of its activity at 70 °C for an hour and a half. No significant effect on Blg29 was observed when incubated with metal ions except for a small increase with ion Ca<sup>2+</sup>. Blg29 showed high substrate activity towards lichenan where <em>V</em><sub>m</sub>, <em>K</em><sub>m</sub>, <em>K</em><sub>cat,</sub> and <em>k</em><sub>cat</sub>/<em>K</em><sub>m</sub> values were 2040.82 μmolmin<sup>‾1</sup>mg<sup>‾1</sup>, 4.69 mg/mL, and 986.39 s‾<sup>1</sup> and 210.32 mLs<sup>‾1</sup>mg‾<sup>1</sup> respectively. The high thermostability and activity make this enzyme useable for a broad prospect in industry applications.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106486"},"PeriodicalIF":1.6,"publicationDate":"2024-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140633196","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Design and construction of a phage-displayed Camelid nanobody library using a simple bioinformatics method 用简单的生物信息学方法设计和构建噬菌体显示的驼科纳米抗体库

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-18 DOI: 10.1016/j.pep.2024.106485

Aliasghar Rahimian , Ali Nabati , Hooman Askari , Mohammad Saffarioun , Mahdi Aminian

{"title":"Design and construction of a phage-displayed Camelid nanobody library using a simple bioinformatics method","authors":"Aliasghar Rahimian , Ali Nabati , Hooman Askari , Mohammad Saffarioun , Mahdi Aminian","doi":"10.1016/j.pep.2024.106485","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106485","url":null,"abstract":"<div><h3>Background</h3><p>Rational design of synthetic phage-displayed libraries requires the identification of the most appropriate positions for randomization using defined amino acid sets to recapitulate the natural occurrence. The present study uses position-specific scoring matrixes (PSSMs) for identifying and randomizing Camelidae nanobody (VHH) CDR3. The functionality of a synthetic VHH repertoire designed by this method was tested for discovering new VHH binders to recombinant coagulation factor VII (rfVII).</p></div><div><h3>Methods</h3><p>Based on PSSM analysis, the CDR3 of cAbBCII10 VHH framework was identified, and a set of amino acids for the substitution of each PSSM-CDR3 position was defined. Using the Rosetta design SwiftLib tool, the final repertoire was back-translated to a degenerate nucleotide sequence. A synthetic phage-displayed library was constructed based on this repertoire and screened for anti-rfVII binders.</p></div><div><h3>Results</h3><p>A synthetic phage-displayed VHH library with 1 × 10<sup>8</sup> variants was constructed. Three VHH binders to rfVII were isolated from this library with estimated dissociation constants (K<sub>D</sub>) of 1 × 10<sup>−8</sup> M, 5.8 × 10<sup>−8</sup> M and 2.6 × 10<sup>-</sup><sup>7</sup> M.</p></div><div><h3>Conclusion</h3><p>PSSM analysis is a simple and efficient way to design synthetic phage-displayed libraries.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106485"},"PeriodicalIF":1.6,"publicationDate":"2024-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140647084","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Alocasia macrorrhiza rhizome lectin inhibits growth of pathogenic bacteria and human lung cancer cell in vitro and Ehrlich ascites carcinoma cell in vivo in mice 大根藻根茎凝集素可抑制致病菌、体外人类肺癌细胞和体内小鼠艾氏腹水癌细胞的生长

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-16 DOI: 10.1016/j.pep.2024.106484

Hossain Mohammad Hridoy , Md Pervez Hossain , Md Hasan Ali , Imtiaj Hasan , Md Belal Uddin , Mohammad Taufiq Alam , Syed Rashel Kabir

{"title":"Alocasia macrorrhiza rhizome lectin inhibits growth of pathogenic bacteria and human lung cancer cell in vitro and Ehrlich ascites carcinoma cell in vivo in mice","authors":"Hossain Mohammad Hridoy , Md Pervez Hossain , Md Hasan Ali , Imtiaj Hasan , Md Belal Uddin , Mohammad Taufiq Alam , Syed Rashel Kabir","doi":"10.1016/j.pep.2024.106484","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106484","url":null,"abstract":"<div><p>Cancer and antibiotic resistance represent significant global challenges, affecting public health and healthcare systems worldwide. Lectin, a carbohydrate-binding protein, displays various biological properties, including antimicrobial and anticancer activities. This study focused on anticancer and antibacterial properties of <em>Alocasia macrorrhiza</em> lectin (AML). AML, with a molecular weight of 11.0 ± 1.0 kDa was purified using Ion-exchange chromatography, and the homotetrameric form was detected by gel-filtration chromatography. It agglutinates mouse erythrocytes, that was inhibited by 4-Nitrophenyl-α-<span>d</span>-mannopyranoside. Maximum hemagglutination activity was observed below 60 °C and within a pH range from 8 to 11. Additionally, it exhibited moderate toxicity against brine shrimp nauplii with LD<sub>50</sub> values of 321 μg/ml and showed antibacterial activity against <em>Escherichia coli</em> and <em>Shigella dysenteriae</em>. <em>In vitro</em> experiments demonstrated that AML suppressed the proliferation of mice Ehrlich ascites carcinoma (EAC) cells by 35 % and human lung cancer (A549) cells by 40 % at 512 μg/ml concentration. <em>In vivo</em> experiments involved intraperitoneal injection of AML in EAC-bearing mice for five consecutive days at doses of 2.5 and 5.0 mg/kg/day, and the results indicated that AML inhibited EAC cell growth by 37 % and 54 %, respectively. Finally, it can be concluded that AML can be used for further anticancer and antibacterial studies.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106484"},"PeriodicalIF":1.6,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140558240","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Alternative strategies for the recombinant synthesis, DOPA modification and analysis of mussel foot proteins – A case study for Mefp-3 from Mytilus edulis 贻贝足蛋白质重组合成、DOPA修饰和分析的替代策略--贻贝Mefp-3的案例研究

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-10 DOI: 10.1016/j.pep.2024.106483

Constanze Zwies , Ángela María Vargas Rodríguez , Marcel Naumann , Franziska Seifert , Markus Pietzsch

{"title":"Alternative strategies for the recombinant synthesis, DOPA modification and analysis of mussel foot proteins – A case study for Mefp-3 from Mytilus edulis","authors":"Constanze Zwies , Ángela María Vargas Rodríguez , Marcel Naumann , Franziska Seifert , Markus Pietzsch","doi":"10.1016/j.pep.2024.106483","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106483","url":null,"abstract":"<div><p>Mussel foot proteins (Mfps) possess unique binding properties to various surfaces due to the presence of L-3,4-dihydroxyphenylalanine (DOPA). <em>Mytilus edulis</em> foot protein-3 (Mefp-3) is one of several proteins in the byssal adhesive plaque. Its localization at the plaque-substrate interface approved that Mefp-3 plays a key role in adhesion. Therefore, the protein is suitable for the development of innovative bio-based binders. However, recombinant Mfp-3s are mainly purified from inclusion bodies under denaturing conditions. Here, we describe a robust and reproducible protocol for obtaining soluble and tag-free Mefp-3 using the SUMO-fusion technology. Additionally, a microbial tyrosinase from <em>Verrucomicrobium spinosum</em> was used for the <em>in vitro</em> hydroxylation of peptide-bound tyrosines in Mefp-3 for the first time. The highly hydroxylated Mefp-3, confirmed by MALDI-TOF-MS, exhibited excellent adhesive properties comparable to a commercial glue. These results demonstrate a concerted and simplified high yield production process for recombinant soluble and tag-free Mfp3-based proteins with on demand DOPA modification.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106483"},"PeriodicalIF":1.6,"publicationDate":"2024-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S104659282400055X/pdfft?md5=d9688fe00176c5d4d32973db47e6eafc&pid=1-s2.0-S104659282400055X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140555386","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Expression, purification, and crystal structure of mpox virus A41 protein mpox 病毒 A41 蛋白的表达、纯化和晶体结构

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-06 DOI: 10.1016/j.pep.2024.106480

Haihai Jiang , Juncheng Li , Yuxin Jian , Tingting Yang , Jin Zhang , Jian Li

{"title":"Expression, purification, and crystal structure of mpox virus A41 protein","authors":"Haihai Jiang , Juncheng Li , Yuxin Jian , Tingting Yang , Jin Zhang , Jian Li","doi":"10.1016/j.pep.2024.106480","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106480","url":null,"abstract":"<div><p>Mpox is a zoonotic disease that was once endemic in Africa countries caused by mpox virus. However, cases recently have been confirmed in many non-endemic countries outside of Africa. The rapidly increasing number of confirmed mpox cases poses a threat to the international community. In-depth studies of key viral factors are urgently needed, which will inform the design of multiple antiviral agents. Mpox virus <em>A41L</em> gene encodes a secreted protein, A41, that is nonessential for viral replication, but could affect the host response to infection via interacting with chemokines. Here, mpox virus A41 protein was expressed in Sf9 cells, and purified by affinity chromatography followed by gel filtration. Surface plasmon resonance spectroscopy showed that purified A41 binds a certain human chemokine CXCL8 with the equilibrium dissociation constant (<em>K</em><sub>D</sub>) being 1.22 × 10<sup>−6</sup> M. The crystal structure of mpox virus A41 protein was solved at 1.92 Å. Structural analysis and comparison revealed that mpox virus A41 protein adopts a characteristic β-sheet topology, showing minor differences with that of vaccinia virus. These preliminary structural and functional studies of A41 protein from mpox virus will help us better understand its role in chemokine subversion, and contributing to the knowledge to viral chemokine binding proteins.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106480"},"PeriodicalIF":1.6,"publicationDate":"2024-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140558241","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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 calcium-binding photoprotein clytin II: Expression of the preferred human codon-optimized clytin II gene in Chinese hamster ovary-K1 cells and its use in the G-protein-coupled receptor assays 钙结合光蛋白 clytin II：在中国仓鼠卵巢-K1 细胞中表达优选的人类密码子优化的 clytin II 基因及其在 G 蛋白偶联受体检测中的应用。

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-05 DOI: 10.1016/j.pep.2024.106481

Satoshi Inouye , Jun-ichi Sato , Yuiko Sahara-Miura , Sunao Hisada

{"title":"The calcium-binding photoprotein clytin II: Expression of the preferred human codon-optimized clytin II gene in Chinese hamster ovary-K1 cells and its use in the G-protein-coupled receptor assays","authors":"Satoshi Inouye , Jun-ichi Sato , Yuiko Sahara-Miura , Sunao Hisada","doi":"10.1016/j.pep.2024.106481","DOIUrl":"10.1016/j.pep.2024.106481","url":null,"abstract":"<div><p>Clytin II (CLII) is a Ca<sup>2+</sup>-binding photoprotein and has been identified as an isotype of clytin I (CLI). CLII consists of apoCLII (an apoprotein) and 2-peroxide of coelenterazine (an adduct of molecular oxygen to coelenterazine), which is identical to the widely used Ca<sup>2+</sup>-binding photoprotein, aequorin (AQ). However, CLII triggered by Ca<sup>2+</sup> exhibits a 4.5-fold higher maximum luminescence intensity (<em>I</em><sub>max</sub>) compared to both AQ and CLI, and it is approximately 5 times less sensitive to Ca<sup>2+</sup> than AQ. To confirm the suitability of the preferred human codon-optimized CLII (pCLII) gene for cell-based G-protein-coupled receptor (GPCR) assays, a transformant stably expressing apoprotein of pCLII using the pCLII gene in the mitochondria of CHO–K1 cells was established and <em>in situ</em> regenerated pCLII in the cells were applied to the high-throughput screening system. An ATP-stimulated GPCR assay for endogenous P2Y purinergic receptors was confirmed using the established stable transformant.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"220 ","pages":"Article 106481"},"PeriodicalIF":1.6,"publicationDate":"2024-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140760159","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Enzymatic characterization and thermostability improvement of an acidophilic endoxylanase PphXyn11 from Paenibacillus physcomitrellae XB 嗜酸性内聚糖酶 PphXyn11 的酶学表征和热稳定性改进

IF 1.6 4区生物学

Protein expression and purification Pub Date : 2024-04-05 DOI: 10.1016/j.pep.2024.106482

Le Wang, Yan Yan Wang, Zhi Ling Chen, Yan Hong Li

{"title":"Enzymatic characterization and thermostability improvement of an acidophilic endoxylanase PphXyn11 from Paenibacillus physcomitrellae XB","authors":"Le Wang, Yan Yan Wang, Zhi Ling Chen, Yan Hong Li","doi":"10.1016/j.pep.2024.106482","DOIUrl":"https://doi.org/10.1016/j.pep.2024.106482","url":null,"abstract":"<div><p>GH11 enzyme is known to be specific and efficient for the hydrolysis of xylan. It has been isolated from many microorganisms, and its enzymatic characteristics and thermostability vary between species. In this study, a GH11 enzyme PphXyn11 from a novel xylan-degrading strain of <em>Paenibacillus physcomitrellae</em> XB was characterized, and five mutants were constructed to try to improve the enzyme's thermostability. The results showed that PphXyn11 was an acidophilic <em>endo</em>-<em>β</em>-1,4-xylanase with the optimal reaction pH of 3.0–4.0, and it could deconstruct different kinds of xylan substrates efficiently, such as beechwood xylan, wheat arabinoxylan and xylo-oligosaccharides, to produce xylobiose and xylotriose as the main products at the optimal reaction temperature of 40 °C. Improvement of the thermal stability of PphXyn11 using site-directed mutagenesis revealed that three mutants, W33C/N47C, S127C/N174C and S49E, designed by adding the disulfide bonds at the <em>N</em>-terminal, <em>C</em>-terminal and increasing the charged residues on the surface of PphXyn11 respectively, could increase the enzymatic activity and thermal stablility significantly and make the optimal reaction temperature reach 50 °C. Molecular dynamics simulations as well as computed the numbers of salt bridges and hydrogen bonds indicated that the protein structures of these three mutants were more stable than the wild type, which provided theoretical support for their improved thermal stability. Certainly, further research is necessary to improve the enzymatic characteristics of PphXyn11 to achieve the bioconversion of hemicellulosic biomass on an applicable scale.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106482"},"PeriodicalIF":1.6,"publicationDate":"2024-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140535023","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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