Amylase - PMC

Dibyajit Lahiri, Moupriya Nag, Ritwik Banerjee, Dipro Mukherjee, Sayantani Garai, Tanmay Sarkar, Ankita Dey, Hassan I. Sheikh, Sushil Kumar Pathak, Hisham Atan Edinur, Siddhartha Pati, Rina Rani Ray

Front Cell Infect Microbiol. 2021; 11: 660048. Published online 2021 Apr 27. doi: 10.3389/fcimb.2021.660048

PMCID:: PMC8112260

Abstract Article PDF–5.1M

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Amylases StAmy23, StBAM1 and StBAM9 regulate cold-induced sweetening of potato tubers in distinct ways

Juan Hou, Huiling Zhang, Jun Liu, Stephen Reid, Tengfei Liu, Shijing Xu, Zhendong Tian, Uwe Sonnewald, Botao Song, Conghua Xie

J Exp Bot. 2017 Apr 1; 68(9): 2317–2331. Published online 2017 Mar 28. doi: 10.1093/jxb/erx076

PMCID:: PMC5447890

Abstract Article PDF–11M

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Native to designed: microbial -amylases for industrial applications

Si Jie Lim, Siti Nurbaya Oslan

PeerJ. 2021; 9: e11315. Published online 2021 May 18. doi: 10.7717/peerj.11315

PMCID:: PMC8139272

Abstract Article PDF–4.2M

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Biochemical Characterization of the Amylase Activity from the New Haloarchaeal Strain Haloarcula sp. HS Isolated in the Odiel Marshlands

Patricia Gómez-Villegas, Javier Vigara, Luis Romero, Cecilia Gotor, Sara Raposo, Brígida Gonçalves, Rosa Léon

Biology (Basel) 2021 Apr; 10(4): 337. Published online 2021 Apr 16. doi: 10.3390/biology10040337

PMCID:: PMC8073556

Abstract Article PDF–5.0M

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Maltooligosaccharides: Properties, Production and Applications

Mária Bláhová, Vladimír Štefuca, Helena Hronská, Michal Rosenberg

Molecules. 2023 Apr; 28(7): 3281. Published online 2023 Apr 6. doi: 10.3390/molecules28073281

PMCID:: PMC10097025

Abstract Article PDF–1.5M

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In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites

Zuzana Janíčková, Štefan Janeček

Molecules. 2021 Sep; 26(18): 5704. Published online 2021 Sep 21. doi: 10.3390/molecules26185704

PMCID:: PMC8467227

Abstract Article PDF–21M

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Structural and functional adaptation in extremophilic microbial α-amylases

Aziz Ahmad, Rahamtullah, Rajesh Mishra

Biophys Rev. 2022 Apr; 14(2): 499–515. Published online 2022 Jan 24. doi: 10.1007/s12551-022-00931-z

PMCID:: PMC9043155

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Promoter-proximal introns impact recombinant amylase expression in Saccharomyces cerevisiae

Kirstie S Schwerdtfeger, Marthinus W Myburgh, Willem H van Zyl, Marinda Viljoen-Bloom

FEMS Yeast Res. 2023; 23: foad047. Published online 2023 Oct 27. doi: 10.1093/femsyr/foad047

PMCID:: PMC10647015

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Toward a More Comprehensive View of α-Amylase across Decapods Crustaceans

Leandro Rodríguez-Viera, Daniel Alpízar-Pedraza, Juan Miguel Mancera, Erick Perera

Biology (Basel) 2021 Oct; 10(10): 947. Published online 2021 Sep 22. doi: 10.3390/biology10100947

PMCID:: PMC8533441

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Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance

Christian Roth, Olga V. Moroz, Johan P. Turkenburg, Elena Blagova, Jitka Waterman, Antonio Ariza, Li Ming, Sun Tianqi, Carsten Andersen, Gideon J. Davies, Keith S. Wilson

Int J Mol Sci. 2019 Oct; 20(19): 4902. Published online 2019 Oct 3. doi: 10.3390/ijms20194902

PMCID:: PMC6801514

Abstract Article PDF–5.0M

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Multi-copy alpha-amylase genes are crucial for Ditylenchus destructor to parasitize the plant host

Ling Chen, Mengci Xu, Chunxiao Wang, Jinshui Zheng, Guoqiang Huang, Feng Chen, Donghai Peng, Ming Sun

PLoS One. 2020; 15(10): e0240805. Published online 2020 Oct 26. doi: 10.1371/journal.pone.0240805

PMCID:: PMC7588122

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Diverse activities and biochemical properties of amylase and proteases from six freshwater fish species

Chamaiporn Champasri, Suthathip Phetlum, Chanakan Pornchoo

Sci Rep. 2021; 11: 5727. Published online 2021 Mar 11. doi: 10.1038/s41598-021-85258-7

PMCID:: PMC7970969

Abstract Article PDF–1.5M

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Biotechnological Processes in Microbial Amylase Production

Subash C. B. Gopinath, Periasamy Anbu, M. K. Md Arshad, Thangavel Lakshmipriya, Chun Hong Voon, Uda Hashim, Suresh V. Chinni

Biomed Res Int. 2017; 2017: 1272193. Published online 2017 Feb 9. doi: 10.1155/2017/1272193

PMCID:: PMC5322433

Abstract Article PDF–1.9M

Select item 815071016.

Statistical Based Bioprocess Design for Improved Production of Amylase from Halophilic Bacillus sp. H7 Isolated from Marine Water

J. N. Bandal, V. A. Tile, R. Z. Sayyed, H. P. Jadhav, N. I. Wan Azelee, Subhan Danish, Rahul Datta

Molecules. 2021 May; 26(10): 2833. Published online 2021 May 11. doi: 10.3390/molecules26102833

PMCID:: PMC8150710

Abstract Article PDF–2.5M

Select item 1038411317.

Structural and Functional Characterization of Drosophila melanogaster α-Amylase

Moez Rhimi, Jean-Luc Da Lage, Richard Haser, Georges Feller, Nushin Aghajari

Molecules. 2023 Jul; 28(14): 5327. Published online 2023 Jul 11. doi: 10.3390/molecules28145327

PMCID:: PMC10384113

Abstract Article PDF–5.2M

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Amylase production from marine sponge Hymeniacidon perlevis; potentials sustainability benefits

Praise Tochukwu Nnaji, Emmanuel Adukwu, H. Ruth Morse, Rachael U. Chidugu-Ogborigbo

PLoS One. 2023; 18(12): e0294931. Published online 2023 Dec 21. doi: 10.1371/journal.pone.0294931

PMCID:: PMC10734944

Abstract Article PDF–1.4M

Select item 1067168219.

Natural Inhibitors of Mammalian α-Amylases as Promising Drugs for the Treatment of Metabolic Diseases

Aleksandr P. Kalinovskii, Oksana V. Sintsova, Irina N. Gladkikh, Elena V. Leychenko

Int J Mol Sci. 2023 Nov; 24(22): 16514. Published online 2023 Nov 20. doi: 10.3390/ijms242216514

PMCID:: PMC10671682

Abstract Article PDF–2.6M

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Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (Taka-amylase)

Christine L. Gee, James. M. Holton, Alexander McPherson

J Biosci Bioeng. Author manuscript; available in PMC 2022 Jun 1.

Published in final edited form as: J Biosci Bioeng. 2021 Jun; 131(6): 605–612. Published online 2021 Apr 2. doi: 10.1016/j.jbiosc.2021.02.008

PMCID:: PMC8187280

Abstract Article PDF–2.0M

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Figure 1Optimization and purification conditions of amylase enzyme from selected Bacillus sp.

(A) The effect of temperature. B. megaterium, B. subtilis, and B. cereus showed maximum amylase production at 45 °C, while other isolates showed maximum amylase production at 55 °C. (B) The effect of incubation time. All isolates showed maximum amylase production after 24 h incubation. (C) The effect of pH. All Bacillus isolates showed maximum amylase production at a pH of 8.0 except B. subtilis, which maximally produced amylase at a pH of 7.0. (D) The effect of starch concentration. B. subtilis and B. cereus had maximum amylase production at 1.5% soluble starch concentration. The remaining isolates had maximum amylase production at 2.0% soluble starch concentration.

Optimizing and purifying extracellular amylase from soil bacteria to inhibit clinical biofilm-forming bacteria

PeerJ. 2020;8:e10288.
Figure 5.SDS-PAGE Analysis of Partially Purified Amylase

Lane1, Molecular mass marker; Lane2, partial purified amylase from SS2; Lane3, partial purified amylase from SS1; Lane4, partial purified amylase from SS3.

Characterizing Novel Thermophilic Amylase Producing Bacteria From Taptapani Hot Spring, Odisha, India

Jundishapur J Microbiol. 2014 Dec;7(12):e11800.
Figure 1.

Kaplan-Meier survival curves of pleural amylase levels ≥75 IU/L and <75 IU/L. (A) Among all patients, 125 had an amylase level of ≥75 IU/L, and 237 had an amylase level of <75 IU/L. The curve for an amylase level of ≥75 IU/L was under the curve for an amylase level of <75 IU/L and showed a significantly decreased mortality [log-rank test p<0.001, HR 0.54 (95% CI: 0.41-0.71)]. (B) Among patients with lung cancer, 117 had an amylase level of ≥75 IU/L, and 183 had an amylase level of <75 IU/L. The curve for an amylase level of ≥75 IU/L was under the curve for an amylase level of <75 IU/L and showed a significantly decreased mortality [log-rank test p<0.001, HR 0.47 (95% CI: 0.35-0.62)]. HR: hazard ratio, CI: confidence interval

Differences in Pleural Fluid Amylase Levels in Patients with Malignant Pleural Effusion Based on Cancer Type, Histologic Type, and Epidermal Growth Factor Receptor Mutations

Intern Med. 2023 Dec 15;62(24):3601-3607.
Figure 3SDS-PAGE amylase profile for B. alvei and B. cereus.

Lane 1: molecular weight marker. Lane 2: amylase purified from B. alvei; Lane 3: amylase purified from B. cereus.

Optimizing and purifying extracellular amylase from soil bacteria to inhibit clinical biofilm-forming bacteria

PeerJ. 2020;8:e10288.

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Amylase (89938)
PMC
glutamate synthase 1 [Arabidopsis thaliana]
glutamate synthase 1 [Arabidopsis thaliana]
gi|18414469|ref|NP_568134.1|

Protein
Micromonospora cremea partial 16S rRNA gene, type strain CR30T
Micromonospora cremea partial 16S rRNA gene, type strain CR30T
gi|307343111|emb|FN658654.1|

Nucleotide
Agromyces salentinus strain 20-5 16S ribosomal RNA gene, partial sequence
Agromyces salentinus strain 20-5 16S ribosomal RNA gene, partial sequence
gi|45934291|gb|AY507129.1|

Nucleotide
Streptomyces variabilis strain NRRL B-3984 DNA-directed RNA polymerase beta subu...
Streptomyces variabilis strain NRRL B-3984 DNA-directed RNA polymerase beta subunit (rpoB) gene, partial cds
gi|1051346483|gb|KT389063.1|

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