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  1. Article ; Online: Simultaneous improvement of thermostability and maltotriose-forming ability of a fungal α-amylase for bread making by directed evolution.

    Wang, Yu-Chuan / Ma, Jun-Wen / Liu, Hai-Jie / Jiang, Zheng-Qiang / Li, Yan-Xiao

    International journal of biological macromolecules

    2024  Volume 264, Issue Pt 1, Page(s) 130481

    Abstract: For applications in food industries, a fungal α-amylase from Malbranchea cinnamomea was engineered by directed evolution. Through two rounds of screening, a mutant α-amylase (mMcAmyA) was obtained with higher optimal temperature (70 °C, 5 °C increase) ... ...

    Abstract For applications in food industries, a fungal α-amylase from Malbranchea cinnamomea was engineered by directed evolution. Through two rounds of screening, a mutant α-amylase (mMcAmyA) was obtained with higher optimal temperature (70 °C, 5 °C increase) and better hydrolysis properties (18.6 % maltotriose yield, 2.5-fold increase) compared to the wild-type α-amylase (McAmyA). Site-directed mutations revealed that Threonine (Thr) 226 Serine (Ser) substitution was the main reason for the property evolution of mMcAmyA. Through high cell density fermentation, the highest expression level of Thr226Ser was 3951 U/mL. Thr226Ser was further used for bread baking with a dosage of 1000 U/kg flour, resulting in a 17.8 % increase in specific volume and a 35.6 % decrease in hardness compared to the control. The results were a significant improvement on those of McAmyA. Moreover, the mutant showed better anti-staling properties compared to McAmyA, as indicated by the improved sensory evaluation after 4 days of storage at 4 and 25 °C. These findings provide insights into the structure-function relationship of fungal α-amylase and introduce a potential candidate for bread-making industry.
    MeSH term(s) alpha-Amylases/genetics ; alpha-Amylases/metabolism ; Bread ; Hydrolysis ; Trisaccharides
    Chemical Substances alpha-Amylases (EC 3.2.1.1) ; maltotriose (639K0T34IK) ; Trisaccharides
    Language English
    Publishing date 2024-02-29
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2024.130481
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: High-level expression of a glycoside hydrolase family 26 β-mannanase from Aspergillus niger in Pichia pastoris for production of partially hydrolysed fenugreek gum

    Wang, Nan-Nan / Liu, Jun / Li, Yan-Xiao / Ma, Jun-Wen / Yan, Qiao-Juan / Jiang, Zheng-Qiang

    Process biochemistry. 2021 Jan., v. 100

    2021  

    Abstract: A codon-optimised β-mannanase gene from Aspergillus niger (AnMan26) was heterologously expressed in Pichia pastoris. The peak enzyme activity of 22,100 U mL⁻¹ was achieved in a 5-L fermenter. AnMan26 was purified to homogeneity with 1.6-fold purification ...

    Abstract A codon-optimised β-mannanase gene from Aspergillus niger (AnMan26) was heterologously expressed in Pichia pastoris. The peak enzyme activity of 22,100 U mL⁻¹ was achieved in a 5-L fermenter. AnMan26 was purified to homogeneity with 1.6-fold purification via Sephacryl S100 HR gel filtration. It exhibited optimal activity at pH 5.0 and 45 °C. AnMan26 was stable within the pH range 2.5–7.0 and exhibited good thermostability up to 40 °C. Moreover, it revealed highest specific activity of 2869.0 U mg⁻¹ towards locust bean gum, and efficiently degraded various mannans to manno-oligosaccharides and hydrolysed mannotetraose and mannopentaose. Furthermore, AnMan26 hydrolysed fenugreek gum to yield partially hydrolysed fenugreek gum (PHFG) with the weight-average molecular weight of 1.8 × 10³ Da. The hydrolysis ratio of galactomannan in fenugreek gum was 82.2 %. Thus, an effective β-mannanase for PHFG production was produced in this study.
    Keywords Aspergillus niger ; Komagataella pastoris ; enzyme activity ; fenugreek ; fermenters ; galactomannans ; gel chromatography ; genes ; glycosides ; hydrolysis ; locust bean gum ; molecular weight ; pH ; thermal stability
    Language English
    Dates of publication 2021-01
    Size p. 90-97.
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean
    ISSN 1359-5113
    DOI 10.1016/j.procbio.2020.09.034
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: High-level expression of a novel α-amylase from Thermomyces dupontii in Pichia pastoris and its application in maltose syrup production.

    Wang, Yu-Chuan / Zhao, Ning / Ma, Jun-Wen / Liu, Jun / Yan, Qiao-Juan / Jiang, Zheng-Qiang

    International journal of biological macromolecules

    2019  Volume 127, Page(s) 683–692

    Abstract: A novel α-amylase gene (TdAmyA) with an open reading frame of 1431 bp, deducing 476 amino acids, was cloned from the thermophilic fungus Thermomyces dupontii L18. The recombinant α-amylase was successfully over-expressed in Pichia pastoris. The highest α- ...

    Abstract A novel α-amylase gene (TdAmyA) with an open reading frame of 1431 bp, deducing 476 amino acids, was cloned from the thermophilic fungus Thermomyces dupontii L18. The recombinant α-amylase was successfully over-expressed in Pichia pastoris. The highest α-amylase activity of 38,314 U/mL was obtained with protein content of 28.7 mg/mL after 168 h high-cell density fermentation. Molecular mass of purified TdAmyA was 61.2 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 59.2 kDa by gel filtration. TdAmyA was a glycoprotein with 5.3% (w/w) of carbohydrate. TdAmyA exhibited maximal activity at 60 °C and pH 6.5, and was thermostable up to 55 °C within pH 4.5-10.0. It was more active towards linear starchy substrates than branched ones. The hydrolysis products were mainly comprised of maltose and maltotriose. TdAmyA produced the highest maltose content of 51.8% after 8 h hydrolysis. Thus, TdAmyA might be a candidate α-amylase for maltose syrup production.
    MeSH term(s) Fungal Proteins/biosynthesis ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Maltose/chemistry ; Pichia/genetics ; Pichia/metabolism ; Recombinant Proteins/blood ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Starch/chemistry ; Trisaccharides/chemistry ; alpha-Amylases/biosynthesis ; alpha-Amylases/chemistry ; alpha-Amylases/genetics
    Chemical Substances Fungal Proteins ; Recombinant Proteins ; Trisaccharides ; maltotriose (639K0T34IK) ; Maltose (69-79-4) ; Starch (9005-25-8) ; alpha-Amylases (EC 3.2.1.1)
    Language English
    Publishing date 2019-01-29
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2019.01.162
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  4. Article ; Online: Fractalkine/CX3CR1 axis modulated the development of pancreatic ductal adenocarcinoma via JAK/STAT signaling pathway.

    Huang, LiYa / Ma, BinWu / Ma, JunWen / Wang, Feng

    Biochemical and biophysical research communications

    2017  Volume 493, Issue 4, Page(s) 1510–1517

    Abstract: Pancreatic ductal adenocarcinoma (PDAC) is a fatal malignancy with an estimated 5 year survival rate of approximately 5% of all stages combined. High potential of PDAC metastasis is a leading cause for high mortality and poor prognosis. The majority of ... ...

    Abstract Pancreatic ductal adenocarcinoma (PDAC) is a fatal malignancy with an estimated 5 year survival rate of approximately 5% of all stages combined. High potential of PDAC metastasis is a leading cause for high mortality and poor prognosis. The majority of patients present with distant metastasis at diagnosis. Fractalkine (FKN) is recognized as a chemokine and a specific ligand of CX3CR1. It has been reported that FKN/CX3CR1 system was upregulated in many types of solid tumors. However, role of FKN/CX3CR1 in PDAC development remains unclear. In the current investigation, we found that FKN and CX3CR1 expression was significantly increased in PDAC tissues, especially in the metastatic samples, and was highly-correlated with severity of PDAC. Ectopic expression of FKN promoted the proliferation and migration of PDAC, while knockdown of CX3CR1 reversed the function of FKN. In addition, PDAC cells with FKN-deficiency showed impaired proliferation and migration activity. The underlying mechanism is that FKN/CX3CR1 activated JAK/STAT signaling, which in turn regulated cell growth. Consistently, in vivo tumorigenesis assay validated the regulatory role of FKN/CX3CR1 in PDAC growth. Our investigation helped understanding the pathogenesis of PDAC occurrence, and demonstrated critical role of FKN/CX3CR1 in PDAC development.
    MeSH term(s) Animals ; CX3C Chemokine Receptor 1 ; Carcinoma, Pancreatic Ductal/genetics ; Carcinoma, Pancreatic Ductal/metabolism ; Carcinoma, Pancreatic Ductal/secondary ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Chemokine CX3CL1/antagonists & inhibitors ; Chemokine CX3CL1/genetics ; Chemokine CX3CL1/metabolism ; Gene Knockdown Techniques ; Humans ; Janus Kinases/metabolism ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Pancreatic Neoplasms/etiology ; Pancreatic Neoplasms/genetics ; Pancreatic Neoplasms/metabolism ; RNA Interference ; Receptors, Chemokine/antagonists & inhibitors ; Receptors, Chemokine/genetics ; Receptors, Chemokine/metabolism ; STAT Transcription Factors/metabolism ; Signal Transduction
    Chemical Substances CX3C Chemokine Receptor 1 ; CX3CL1 protein, human ; CX3CR1 protein, human ; Chemokine CX3CL1 ; Receptors, Chemokine ; STAT Transcription Factors ; Janus Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2017-12-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.10.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 116: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  5. Article: High-level expression of a novel α-amylase from Thermomyces dupontii in Pichia pastoris and its application in maltose syrup production

    Wang, Yu-chuan / Zhao, Ning / Ma, Jun-wen / Liu, Jun / Yan, Qiao-juan / Jiang, Zheng-qiang

    International journal of biological macromolecules. 2019 Apr. 15, v. 127

    2019  

    Abstract: A novel α-amylase gene (TdAmyA) with an open reading frame of 1431 bp, deducing 476 amino acids, was cloned from the thermophilic fungus Thermomyces dupontii L18. The recombinant α-amylase was successfully over-expressed in Pichia pastoris. The highest α- ...

    Abstract A novel α-amylase gene (TdAmyA) with an open reading frame of 1431 bp, deducing 476 amino acids, was cloned from the thermophilic fungus Thermomyces dupontii L18. The recombinant α-amylase was successfully over-expressed in Pichia pastoris. The highest α-amylase activity of 38,314 U/mL was obtained with protein content of 28.7 mg/mL after 168 h high-cell density fermentation. Molecular mass of purified TdAmyA was 61.2 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 59.2 kDa by gel filtration. TdAmyA was a glycoprotein with 5.3% (w/w) of carbohydrate. TdAmyA exhibited maximal activity at 60 °C and pH 6.5, and was thermostable up to 55 °C within pH 4.5–10.0. It was more active towards linear starchy substrates than branched ones. The hydrolysis products were mainly comprised of maltose and maltotriose. TdAmyA produced the highest maltose content of 51.8% after 8 h hydrolysis. Thus, TdAmyA might be a candidate α-amylase for maltose syrup production.
    Keywords Pichia pastoris ; Thermomyces ; alpha-amylase ; amino acids ; enzyme activity ; fermentation ; gel chromatography ; genes ; glycoproteins ; hydrolysis ; maltose ; maltotriose ; molecular weight ; open reading frames ; pH ; polyacrylamide gel electrophoresis ; protein content ; syrups ; thermal stability ; thermophilic fungi
    Language English
    Dates of publication 2019-0415
    Size p. 683-692.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2019.01.162
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

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  6. Article: A novel high maltose-forming α-amylase from Rhizomucor miehei and its application in the food industry

    Wang, Yu-chuan / Hu, Hui-fang / Ma, Jun-wen / Yan, Qiao-juan / Liu, Hai-jie / Jiang, Zheng-qiang

    Food chemistry. 2019 Aug. 28,

    2019  

    Abstract: A novel α-amylase gene (RmAmyA) from Rhizomucor miehei was cloned and expressed in Pichia pastoris. RmAmyA showed 70% amino acid identity with the α-amylase obtained from Rhizomucor pusillus. A high α-amylase activity of 29,794.2 U/mL was found through ... ...

    Abstract A novel α-amylase gene (RmAmyA) from Rhizomucor miehei was cloned and expressed in Pichia pastoris. RmAmyA showed 70% amino acid identity with the α-amylase obtained from Rhizomucor pusillus. A high α-amylase activity of 29,794.2 U/mL was found through high cell density fermentation. The molecular mass of RmAmyA was determined to be 49.9 kDa via SDS-PAGE. RmAmyA was optimally active at 75 °C and pH 6.0, and it did not require Ca2+ to improve its activity. It exhibited broad substrate specificity towards amylose, amylopectin, soluble starch, pullulan, and cyclodextrins. High level of maltose (54%, w/w) was produced after liquefied starch was hydrolysed with RmAmyA for 16 h. Moreover, the addition of RmAmyA into Chinese steamed bread resulted in 7.7% increment in the specific volume, and 17.2% and 11.5% reduction in the chewiness and hardness, respectively. These results indicate that RmAmyA might be a potential candidate for applications in the food industry.
    Keywords Komagataella pastoris ; Rhizomucor miehei ; Rhizomucor pusillus ; alpha-amylase ; amino acids ; amylopectin ; amylose ; breads ; calcium ; chewiness ; cyclodextrins ; enzyme activity ; fermentation ; food industry ; genes ; hardness ; hydrolysis ; maltose ; molecular weight ; pH ; polyacrylamide gel electrophoresis ; pullulan ; substrate specificity
    Language English
    Dates of publication 2019-0828
    Publishing place Elsevier Ltd
    Document type Article
    Note Pre-press version
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2019.125447
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  7. Article ; Online: A novel high maltose-forming α-amylase from Rhizomucor miehei and its application in the food industry.

    Wang, Yu-Chuan / Hu, Hui-Fang / Ma, Jun-Wen / Yan, Qiao-Juan / Liu, Hai-Jie / Jiang, Zheng-Qiang

    Food chemistry

    2019  Volume 305, Page(s) 125447

    Abstract: A novel α-amylase gene (RmAmyA) from Rhizomucor miehei was cloned and expressed in Pichia pastoris. RmAmyA showed 70% amino acid identity with the α-amylase from Rhizomucor pusillus. A high α-amylase activity of 29,794.2 U/mL was found through high cell ... ...

    Abstract A novel α-amylase gene (RmAmyA) from Rhizomucor miehei was cloned and expressed in Pichia pastoris. RmAmyA showed 70% amino acid identity with the α-amylase from Rhizomucor pusillus. A high α-amylase activity of 29,794.2 U/mL was found through high cell density fermentation. The molecular mass of RmAmyA was determined to be 49.9 kDa via SDS-PAGE. RmAmyA was optimally active at 75 °C and pH 6.0, and it did not require Ca
    MeSH term(s) Bread/analysis ; Food Industry ; Hydrogen-Ion Concentration ; Hydrolysis ; Maltose/metabolism ; Pichia/metabolism ; Rhizomucor/enzymology ; Starch/metabolism ; Substrate Specificity ; Temperature ; alpha-Amylases/chemistry ; alpha-Amylases/genetics ; alpha-Amylases/metabolism
    Chemical Substances Maltose (69-79-4) ; Starch (9005-25-8) ; alpha-Amylases (EC 3.2.1.1)
    Language English
    Publishing date 2019-08-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2019.125447
    Database MEDical Literature Analysis and Retrieval System OnLINE

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