Cited by 23Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationBiofuel production and bioconversion

The DOI matches its Crossref record.

Starches from different sources hydrolysis using a new thermo-tolerant amylase complex produced by Bacillus subtilis T41a: Characterization and efficiency evaluation

Abstract

Bacillus subtilis T41a, an amylase-producing bacterium, was isolated from wheat phylosphere. The optimum catalytic activity and affinity toward different starch types hydrolysis were studied. Response surface methodology was applied to investigate the optimum catalytic conditions. The results indicated that the optimum conditions for enzyme activity were 58 °C and pH 7.2. The enzyme complex was thermostable, retaining almost 50% of its original activity after being kept at 60 °C for 1.5 h. Furthermore, the temperature stability test showed that it was stable at 40 °C for 48 h. Moreover, it was quite stable in a wide pH range of 5–9. Also, the enzyme efficiency in hydrolysing different starches was demonstrated more affinity toward potato starch. The hydrolysis rate recorded over 9 h for 10% substrate concentration of potato, corn and wheat starches were 41, 39 and 38% respectively. AFM images of hydrolyzed starches established similar pattern for potato and corn starches while different surficial morphology in case of wheat starch has been observed. Hence, the B. subtilis T41a amylase complex, as a thermo-tolerant amylase with a good ability to hydrolyze starch can be considered as an interesting and economical candidate for industrial application.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.lwt.2019.05.116

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 35

  1. Ahmed, 2016, Characterization and valuable applications of xylanase from endophytic fungus Aspergillus terreus KP900973 isolated from Corchorus olitorius, Biocatalysis and agricultural biotechnology, 7, 134, 10.1016/j.bcab.2016.05.015 · DOI
  2. Alkando, 2011, A potential new isolate for the production of a thermostable extracellular α-amylase, Journal of Bacteriology Research, 3, 129
  3. An, 2008, Effects of heating modes and sources on nanostructure of gelatinized starch molecules using atomic force microscopy, LWT-Food Science and Technology, 41, 1466, 10.1016/j.lwt.2007.08.026 · DOI
  4. Carvalho, 2008, Properties of an amylase from thermophilic Bacillus SP, Brazilian Journal of Microbiology, 39, 102, 10.1590/S1517-83822008000100023 · DOI
  5. Deb, 2013, Production and partial characterization of extracellular amylase enzyme from Bacillus amyloliquefaciens P-001, SpringerPlus, 2, 154, 10.1186/2193-1801-2-154 · DOI
  6. Dhital, 2017, Mechanisms of starch digestion by α-amylase—structural basis for kinetic properties, Critical Reviews in Food Science and Nutrition, 57, 875, 10.1080/10408398.2014.922043 · DOI
  7. Gupta, 2003, Microbial α-amylases: A biotechnological perspective, Process Biochemistry, 38, 1599, 10.1016/S0032-9592(03)00053-0 · DOI
  8. Hashemi, 2013, Comparison of submerged and solid state fermentation systems effects on the catalytic activity of Bacillus sp. KR-8104 α-amylase at different pH and temperatures, Industrial Crops and Products, 43, 661, 10.1016/j.indcrop.2012.08.002 · DOI
  9. Hashemi, 2015, Different catalytic behavior of α-amylase in response to the nitrogen substance used in the production phase, Journal of Industrial and Engineering Chemistry, 21, 772, 10.1016/j.jiec.2014.04.011 · DOI
  10. Kasprzak, 2012, Effect of enzymatic treatment of different starch sources on the in vitro rate and extent of starch digestion, International Journal of Molecular Sciences, 13, 929, 10.3390/ijms13010929 · DOI
  11. Keharom, 2016, The optimization study of α-amylase activity based on central composite design-response surface methodology by dinitrosalicylic acid method, International Food Research Journal, 23
  12. Konsula, 2004, Hydrolysis of starches by the action of an α-amylase from Bacillus subtilis, Process Biochemistry, 39, 1745, 10.1016/j.procbio.2003.07.003 · DOI · Paper page
  13. Lee, 2017, Evaluation of enzymatic deinking of non-impact ink laser-printed paper using crude enzyme from Penicillium rolfsii c3-2 (1) IBRL, Applied Biochemistry and Biotechnology, 181, 451, 10.1007/s12010-016-2223-4 · DOI
  14. Lévêque, 2000, Thermophilic archaeal amylolytic enzymes, Enzyme and Microbial Technology, 26, 3, 10.1016/S0141-0229(99)00142-8 · DOI
  15. Lim, 1993, Location of phosphate esters in a wheat starch phosphate byˆ 3ˆ 1P-nuclear magnetic resonance spectroscopy, Cereal Chemistry, 70
  16. Maity, 2015, Optimization of solid state fermentation conditions and characterization of thermostable alpha amylase from Bacillus subtilis (ATCC 6633), Journal of Bioprocess & Biotechnology, 5, 1
  17. Mamo, 1999, A highly thermostable amylase from a newly isolated thermophilic Bacillus sp. WN11, Journal of Applied Microbiology, 86, 557, 10.1046/j.1365-2672.1999.00685.x · DOI
  18. Miao, 2018, Microbial starch‐converting enzymes: Recent insights and perspectives, Comprehensive Reviews in Food Science and Food Safety, 17, 1238, 10.1111/1541-4337.12381 · DOI
  19. Moteshafi, 2016, Characterization of produced xylanase by Bacillus subtilis D3d newly isolated from apricot phyllosphere and its potential in pre-digestion of BSG, Journal of Industrial and Engineering Chemistry, 37, 251, 10.1016/j.jiec.2016.03.036 · DOI
  20. Neethirajan, 2012, Ultrastructural analysis of buckwheat starch components using atomic force microscopy, Journal of Food Science, 77, N2, 10.1111/j.1750-3841.2011.02442.x · DOI
  21. Prakash, 2011, Effect of metal ions, EDTA and sulfhydryl reagents on soybean amylase activity, Asian Journal of Biochemistry, 6, 282, 10.3923/ajb.2011.282.290 · DOI
  22. Rasooli, 2008, A thermostable α-amylase producing natural variant of Bacillus spp. isolated from soil in Iran, American Journal of Agricultural and Biological Sciences, 3, 591, 10.3844/ajabssp.2008.591.596 · DOI
  23. Rocky-Salimi, 2016, A novel phytase characterized by thermostability and high pH tolerance from rice phyllosphere isolated Bacillus subtilis BS 46, Journal of Advances Research, 7, 381, 10.1016/j.jare.2016.02.003 · DOI
  24. Sadhu, 2014, Optimization and strain improvement by mutation for enhanced cellulase production by Bacillus sp. (MTCC10046) isolated from cow dung, Journal of King Saud University Science, 26, 323, 10.1016/j.jksus.2014.06.001 · DOI
  25. Soto, 2012, Influence of starch source in the required hydrolysis time for the production of maltodextrins with different dextrose equivalent, African Journal of Biotechnology, 11, 13428
  26. Sujka, 2009, α-Amylolysis of native potato and corn starches–SEM, AFM, nitrogen and iodine sorption investigations, LWT-Food Science and Technology, 42, 1219, 10.1016/j.lwt.2009.01.016 · DOI
  27. Suribabu, 2014, Optimization of physical parameters of alpha amylase producing Brevibacillus borostelensis R1 in submerged fermentation, International Journal of Renewable Energy Technology, 1, 517
  28. Tester, 2006, Hydrolysis of native starches with amylases, Animal Feed Science and Technology, 130, 39, 10.1016/j.anifeedsci.2006.01.016 · DOI
  29. Tiwari, 2014, Enhanced production and characterization of a solvent stable amylase from solvent tolerant Bacillus tequilensis RG-01: Thermostable and surfactant resistant, Science World Journal, 2014
  30. Uthumporn, 2010, Hydrolysis of granular starch at sub-gelatinization temperature using a mixture of amylolytic enzymes, Food and Bioproducts Processing, 88, 47, 10.1016/j.fbp.2009.10.001 · DOI
  31. Vidyalakshmi, 2009, Amylase production on submerged fermentation by Bacillus spp, World Journal of Chemistry, 4, 89
  32. Vieille, 2001, Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability, Microbiology and Molecular Biology Reviews, 65, 1, 10.1128/MMBR.65.1.1-43.2001 · DOI
  33. Wang, 2016, Production of theabrownins using a crude fungal enzyme concentrate, Journal of Biotechnology, 231, 250, 10.1016/j.jbiotec.2016.06.010 · DOI
  34. Yun, 2004, Characterization of a novel amylolytic enzyme encoded by a gene from a soil-derived metagenomic library, Applied and Environmental Microbiology, 70, 7229, 10.1128/AEM.70.12.7229-7235.2004 · DOI
  35. Zhang, 2016, Characterization of A-and B-type starch granules in Chinese wheat cultivars, Journal of Integrative Agriculture, 15, 2203, 10.1016/S2095-3119(15)61305-3 · DOI

Cited by

Sorted by citations

Metadata

Authors
Tavallaie, S., Khomeiri, M., Mousivand, M., Maghsoudlou, Y., & Hashemi, M.
Affiliations
  • Gorgan University of Agricultural Sciences and Natural Resources (IR)
  • Agricultural Research & Education Organization (IR)
Corresponding author
  • Khomeiri, Morteza
  • Hashemi, Maryam
Venue
LWT
Publisher
Elsevier BV
Published
2019-09
Volume
112
Pages
108218
ISSN
0023-6438 (ISSN-L)
OpenAlex
W2947595464
Cited by
23
References
0
Citations by year
2025: 3 · 2024: 1 · 2023: 15 · 2022: 1 · 2021: 3
FWCI
0.54
Type
journal article
Language
en
Open access
closed
Locations
LWT (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
Keywords
amylase, starch hydrolysis, potato starch, corn starch, wheat starch, enzyme stability, enzyme optimization, starch morphology, industrial enzyme applications

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review