ArticlePloS one2015
Purification and characterization of a highly efficient calcium-independent α-amylase from Talaromyces pinophilus 1-95.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 78 citations in OpenAlex.
- Microbial diversity, metabolic properties, and biotechnological prospects of acid-sulfate soils.World journal of microbiology & biotechnology · 2025Review
- Heterologous expression, characterization, and application of recombinant thermostable α-amylase fromBiochemistry and biophysics reports · 2024Article
- Enhanced saccharification levels of corn starch using as a strategy a novel amylolytic complex (AmyHb) from the thermophilic fungus3 Biotech · 2024Article
- Purification and characterization of amylases from three freshwater fish species providing new insight application as enzyme molecular markers for zymography.Fish physiology and biochemistry · 2023Article
- Antimicrobial activity and enzymatic analysis of endophytes isolated from Codonopsis pilosula.FEMS microbiology ecology · 2023Article
- A New Species and Five New Records ofMycobiology · 2023Article
- Production of extracellular amylase contributes to the colonization of Bacillus cereus 0-9 in wheat roots.BMC microbiology · 2022Article
- Characterization of a Novel L-Asparaginase fromFoods (Basel, Switzerland) · 2021Article
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- Article
- Purification and characterization of a noble thermostable algal starch liquefying alpha-amylase fromBiotechnology reports (Amsterdam, Netherlands) · 2020Article
- Catalytic and thermodynamic properties of an acidic α-amylase produced by the fungus3 Biotech · 2020Article
- Purification and characterization of an endo-xylanase from Trichoderma sp., with xylobiose as the main product from xylan hydrolysis.World journal of microbiology & biotechnology · 2019Article
- Aspergillus oryzae S2 AmyA amylase expression in Pichia pastoris: production, purification and novel properties.Molecular biology reports · 2019Article
- Identification of a Novel Transcription Factor TP05746 Involved in Regulating the Production of Plant-Biomass-Degrading Enzymes inFrontiers in microbiology · 2019Article
- A Review on Bioconversion of Agro-Industrial Wastes to Industrially Important Enzymes.Bioengineering (Basel, Switzerland) · 2018Review
- Directly mining a fungal thermostable α-amylase from Chinese Nong-flavor liquor starter.Microbial cell factories · 2018Article
- The transcription factor TpRfx1 is an essential regulator of amylase and cellulase gene expression inBiotechnology for biofuels · 2018Article
- Deletion of TpKu70 facilitates gene targeting in Talaromyces pinophilus and identification of TpAmyR involvement in amylase production.World journal of microbiology & biotechnology · 2017Article
- Genome sequencing and analysis of Talaromyces pinophilus provide insights into biotechnological applications.Scientific reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-amylase is a very important enzyme in the starch conversion process. Most of the α-amylases are calcium-dependent and exhibit poor performance in the simultaneous saccharification and fermentation process of industrial bioethanol production that uses starch as feedstock. In this study, an extracellular amylolytic enzyme was purified from the culture broth of newly isolated Talaromyces pinophilus strain 1-95. The purified amylolytic enzyme, with an apparent molecular weight of 58 kDa on SDS-PAGE, hydrolyzed maltopentaose, maltohexaose, and maltoheptaose into mainly maltose and maltotriose and minor amount of glucose, confirming the endo-acting mode of the enzyme, and hence, was named Talaromyces pinophilus α-amylase (TpAA). TpAA was most active at pH 4.0-5.0 (with the temperature held at 37°C) and 55°C (at pH 5.0), and stable within the pH range of 5.0-9.5 (at 4°C) and below 45°C (at pH 5.0). Interestingly, the Ca2+ did not improve its enzymatic activity, optimal temperature, or thermostability of the enzyme, indicating that the TpAA was Ca2+-independent. TpAA displayed higher enzyme activity toward malto-oligosaccharides and dextrin than other previously reported α-amylases. This highly active Ca2+-independent α-amylase may have potential applications in starch-to-ethanol conversion process.
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