Relevant bibliographies by topics / Α-amylase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Α-amylase'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2025

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Journal articles on the topic "Α-amylase"

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Türker, Celal, and Bahri Devrim Özcan. "Alfa-amilaz Enzimlerini Üreten Termofilik Bacillus Suşlarının İzolasyonu ve Enzimlerin Kısmi Karakterizasyonu." Turkish Journal of Agriculture - Food Science and Technology 3, no. 6 (2015): 387. http://dx.doi.org/10.24925/turjaf.v3i6.387-393.312.

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In the present study, we isolated three thermophilic Bacillus strains from the soil samples collected from the coast sediments of the Burnaz Stream located in Erzin. The isolates were entitled as Bacillus sp. CT1, CT2, and CT3, respectively. The maximum α-amylase production was revealed at 60°C for CT1 strain, and at 80°C for CT2 and CT3 strains, respectively. The optimum enzyme activity was observed at 90°C for CT1 α-amylase, whereas at 60°C for CT2 and CT3 α-amylases. On the other hand, optimum pH value for CT2 α-amylase was 7.0, whereas 8.0 for CT1 and CT3 α-amylases. The specific activitie
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Rebholz, Gerold Felix, Karin Sebald, Sebastian Dirndorfer, Corinna Dawid, Thomas Hofmann та Katharina Anne Scherf. "Impact of exogenous maltogenic α-amylase and maltotetraogenic amylase on sugar release in wheat bread". European Food Research and Technology 247, № 6 (2021): 1425–36. http://dx.doi.org/10.1007/s00217-021-03721-1.

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AbstractThe use of exogenous maltogenic α-amylases or maltotetraogenic amylases of bacterial origin is common in wheat bread production, mainly as antistaling agents to retard crumb firming. To study the impact of maltogenic α-amylase and maltotetraogenic amylase on straight dough wheat bread, we performed a discovery-driven proteomics approach with commercial enzyme preparations and identified the maltotetraogenic amylase P22963 from Pelomonas saccharophila and the maltogenic α-amylase P19531 from Geobacillus stearothermophilus, respectively, as being responsible for the amylolytic activity.
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Zhang, Xiaodong, Caixia Li, Xuantong Chen, Chonlong Chio, Sarita Shrestha, and Wensheng Qin. "Bacillus velezensis Identification and Recombinant Expression, Purification, and Characterization of Its Alpha-Amylase." Fermentation 7, no. 4 (2021): 227. http://dx.doi.org/10.3390/fermentation7040227.

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Amylases account for about 30% of the global market of industrial enzymes, and the current amylases cannot fully meet industrial needs. This study aimed to identify a high α-amylase producing bacterium WangLB, to clone its α-amylase coding gene, and to characterize the α-amylase. Results showed that WangLB belonged to Bacillus velezensis whose α-amylase gene was 1980 bp coding 659 amino acids designated as BvAmylase. BvAmylase was a hydrophilic stable protein with a signal peptide and a theoretical pI of 5.49. The relative molecular weight of BvAmylase was 72.35 kDa, and was verified by SDS-PA
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Mot, René De, та Hubert Verachtert. "Secretion of α-amylase and multiple forms of glucoamylase by the yeast Trichosporon pullulans". Canadian Journal of Microbiology 32, № 1 (1986): 47–51. http://dx.doi.org/10.1139/m86-009.

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Trichosporon pullulans IGC 3488 produced extracellular α-amylase and glucoamylase activities when grown in batches in a medium containing corn steep liquor and soluble starch or corn starch, α-Amylase, unlike glucoamylase activity, was secreted biphasically. For both amylases the maximum concentration was found in stationary phase cultures. The amylolytic enzymes, previously concentrated by ammonium sulfate precipitation, were separated into a glucoamylase fraction and an α-amylase fraction by Ultrogel AcA 54 gel filtration. Pullulanase activity was located in the glucoamylase fraction, wherea
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Melo, Francislete R., Mauricio P. Sales, Lucilene S. Pereira, Carlos Bloch, Octavio L. Franco та Maria B. Ary. "α-Amylase Inhibitors from Cowpea Seeds". Protein & Peptide Letters 6, № 6 (1999): 385–90. http://dx.doi.org/10.2174/092986650606221117144709.

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Abstract: This work describes the first isolation and partial characterization of α-amylase inhibitors from cowpea (Vigna unguiculata) seeds. α-Amylase inhibitors were isolated using an affinity chromatography on Red Sepharose CL-6B. The bound Red Sepharose fraction was active against α-amylases from Bacillus sp., Aspergilus oryzae, V unguicu/ata seeds and also against α-amylases from Callosobruchus maculatus larvae.
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Domingues, Claudia M., and Rosane M. Peralta. "Production of amylase by soil fungi and partial biochemical characterization of amylase of a selected strain (Aspergillus fumigatus Fresenius)." Canadian Journal of Microbiology 39, no. 7 (1993): 681–85. http://dx.doi.org/10.1139/m93-098.

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Filamentous fungi from soil were screened for their ability to produce amylases in semisolid and liquid media with wheat bran. A selected strain identified as Aspergillus fumigatus Fresenius showed high enzymatic activity for α-amylase and glucoamylase. The maximal yield of these amylases was obtained when lignocellulosic materials were the carbon sources. The optimal pH and temperature were 6.0 and 50 °C, respectively, for both enzymes. α-Amylase activity was more thermostable than glucoamylase activity.Key words: amylolitic fungi, α-amylase, glucoamylase, Aspergillus fumigatus.
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Chessa, Jean-Pierre, Georges Feller та Charles Gerday. "Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B". Canadian Journal of Microbiology 45, № 6 (1999): 452–57. http://dx.doi.org/10.1139/w99-021.

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A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other α-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic α-amylase requires both Cl-and Ca2+for i
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Mitsui, Toshiaki, Akihito Ochiai, Hiromoto Yamakawa, Kentaro Kaneko, Aya Kitajima-Koga та Marouane Baslam. "Novel molecular and cell biological insights into function of rice α-amylase". Amylase 2, № 1 (2018): 30–38. http://dx.doi.org/10.1515/amylase-2018-0004.

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Abstract α-Amylases have been of interest in diverse fields for many years because of their importance in basic biology, agriculture, and industry. Starch hydrolysis in plants has been studied extensively in germinating cereal seeds. It is generally accepted that α-amylases are secretory enzymes with a pivotal role in the breakdown of starch reserves in the endosperm. Intriguingly, however, recent investigations reveal that some α-amylases degrade starch in the plastids of living cells. The recent solving of the crystal structure of rice AmyI-1 isoform shows that the binding pocket of starch b
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Rokhati, Nur, Prita Widjajanti, Bambang Pramudono та Heru Susanto. "Performance Comparison of α- and β-Amylases on Chitosan Hydrolysis". ISRN Chemical Engineering 2013 (12 грудня 2013): 1–5. http://dx.doi.org/10.1155/2013/186159.

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The low solubility in common solvent and high viscosity resulting from its high molecular weight (MW) with fiber-like structure prevents a more widespread use of chitosan. This paper presents a performance comparison of nonspecific, commercially available enzymes, α- and β-amylases, for the hydrolysis of chitosan to lower its MW. The results showed that both enzymes demonstrate the ability to be used as catalysts in chitosan hydrolysis with β-amylase having better performance than α-amylase. The chitosan hydrolysis was influenced by not only the enzyme and the chitosan characteristics but also
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Rodríguez-Viera, Leandro, Daniel Alpízar-Pedraza, Juan Miguel Mancera та Erick Perera. "Toward a More Comprehensive View of α-Amylase across Decapods Crustaceans". Biology 10, № 10 (2021): 947. http://dx.doi.org/10.3390/biology10100947.

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Decapod crustaceans are a very diverse group and have evolved to suit a wide variety of diets. Alpha-amylases enzymes, responsible for starch and glycogen digestion, have been more thoroughly studied in herbivore and omnivore than in carnivorous species. We used information on the α-amylase of a carnivorous lobster as a connecting thread to provide a more comprehensive view of α-amylases across decapods crustaceans. Omnivorous crustaceans such as shrimps, crabs, and crayfish present relatively high amylase activity with respect to carnivorous crustaceans. Yet, contradictory results have been o
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Dissertations / Theses on the topic "Α-amylase"

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Thompson, Carl R. "α-Amylase and pullulanase from Thermopallium natronophilum". Thesis, University of Bath, 1998. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300882.

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Shai, LJ, JN Eloff, N. Boaduo, et al. "Yeast alpha glucosidase inhibitory and antioxidant activities of six medicinal plants collected in Phalaborwa, South Africa." Elsevier, 2010. http://encore.tut.ac.za/iii/cpro/DigitalItemViewPage.external?sp=1001248.

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Abstract Recent decades have experienced a sharp increase in the incidence and prevalence of diabetes mellitus. One antidiabetic therapeutic approach is to reduce gastrointestinal glucose production and absorption through the inhibition of carbohydrate-digesting enzymes such as α- amylase and α-glucosidase and α-amylase. The aim of the current study was to screen six medicinal plant species, with alleged antidiabetic properties for α-glucosidase inhibitory activities. Powdered plant materials were extracted with acetone, and tested for ability to inhibit baker's yeast α-glucosidase and α-amyla
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Talamond, Pascale. "Etude de l' α-amylase de lactobacillus fermentum : purification, caractérisation et propriétés. Comparaison avec les α-amylases de Lb. Plantarum et Lb. Manihotivorans". Aix-Marseille 3, 2002. http://www.theses.fr/2002AIX30087.

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Une nouvelle a-amylase de Lb. Fermentum (FERMENTA) obtenue par fermentation à partir de céréales a été purifiée, étudiée au niveau structural et fonctionnel et comparée avec deux autres a-amylases de Lb. Plantarum (PLANTAA) et de Lb. Manihotivorans (MANIHOA). Les trois a-amylases présentent une masse moléculaire voisinant les 100 kDa et des pI du même ordre de grandeur (3,5±0,3). Comme PLANTAA et MANIHOA, la structure de FERMENTA contient des séquences répétées en C-terminal. Les propriétés physico-chimiques (pH 5 et température 40ʿC) ont été déterminées et l'étude cinétique avec l'amylose pou
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Junior, Carlos Bloch. "Studies on α-amylase inhibitors from seeds of Sorghum bicolor". Thesis, Durham University, 1991. http://etheses.dur.ac.uk/6283/.

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Six inhibitors (Slal, SIa2, SIa3, SIa4, SIa5 and SIa6) of α-amylase from mammalian, insect, bacterial and fungal sources were purified from seeds of Sorghum bicolor (L) Moench by saline extraction, precipitation with ammonium sulphate, affinity chromatography on Red Sepharose, preparative and analytical reverse phase HPLC on Vydac C(_18) columns. The complete primary structures of five of these inhibitors (Slal-5) were determined by automatic degradation of the intact, reduced and S-alkylated proteins and by manual DABITC/PITC microsequencing of peptides obtained from enzyme digests. The first
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Brown, Ian. "Pyrococcus furiosus α-amylase as a candidate sterilisation time-temperature integrator". Thesis, University of Birmingham, 2010. http://etheses.bham.ac.uk//id/eprint/1369/.

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Thermal treatment is the most common method used by industry to ensure food is safe for consumption and to increase storage life. To ensure safety, food is often over processed, which can significantly affect its nutritional value as well as taste and flavour attributes. In this study a candidate sterilisation time-temperature integrator (TTI) from the hyperthermophilic Pyrococcus furiosus α-amylase is investigated. Reliability and accuracy of the TTIs was determined by exposure to various isothermal and non-isothermal industrially relevant temperature profiles. The integrated temperature hist
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Gimbi, Dorothy Machunda. "Studies on Properties and Structure of α-Amylase from African Finger Millet". Kyoto University, 2003. http://hdl.handle.net/2433/148322.

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Kyoto University (京都大学)<br>0048<br>新制・課程博士<br>博士(農学)<br>甲第10502号<br>農博第1375号<br>新制||農||881(附属図書館)<br>学位論文||H15||N3857(農学部図書室)<br>UT51-2003-U472<br>京都大学大学院農学研究科応用生命科学専攻<br>(主査)教授 北畠 直文, 教授 小川 正, 教授 伊谷 樹一<br>学位規則第4条第1項該当
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Kosugi, Takahiro. "Theoretical Study of Structural Flexibility and Enzymatic Activity of a Psycrophilic α-Amylase". 京都大学 (Kyoto University), 2012. http://hdl.handle.net/2433/157799.

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Luu, Anh Van, Thi Yen Nguyen, Thi Thuy An Ho, Thi Thanh Hang Nguyen та Truong Giang Nguyen. "Appropriating conditions for acquisition highcontent α – amylase of germinated brown rice variety Oryza stiva Anhdao". Technische Universität Dresden, 2018. https://tud.qucosa.de/id/qucosa%3A33067.

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Brown rice is a food ingredient which has high nutritious values. During germination, some nutritious and functional components are increased such as lysine, vitamin E, B1, B6, magnesium, calcium, iron… and especially γ – amino butyric acid. Enzyme activity will also change during the germination of the grains. The α – amylase activity of ungerminated grains is very low, only 34.91 UI/g. This is because the enzyme is hibernating and not activated. During germination, enzyme activity will increase. Submerge the Anhdao brown glutinous rice for 6 hours at 30oC in solutions with different pH value
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Atkinson, Fiona Suzanne. "The physiological significance of AMY1 gene copy number variation." Thesis, The University of Sydney, 2014. http://hdl.handle.net/2123/13558.

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The AMY1 gene codes for salivary α-amylase (sAA), the enzyme responsible for commencing starch digestion. Humans show unusually high copy number variation (CNV) in AMY1. This thesis examined the potential phenotypic consequences of AMY1 CNV on sAA activity, starch digestion, food intake, and the metabolic responses to starchy foods. Fasting blood and saliva samples, along with anthropometric and dietary intake data, were collected from 201 predominantly young, lean, healthy individuals. AMY1 copy number ranged from 1 – 16 copies, with an average of 6.5 ± 2.6 copies. Individuals with Asian ethn
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Chadha, Vipul. "Oligo-1,6-Glocosidase enzyme of halothermothrix orenii." Thesis, Griffith University, 2012. http://hdl.handle.net/10072/365799.

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Halothermothrix orenii, a gram negative strictly anaerobic thermohalophilic bacterium has been isolated from sediments of a Tunisian salt lake (Chott El Guettar). H. orenii grows optimally at 60˚C with 10% NaCl. Phylogenetically, H. orenii is placed at the base of phylum Firmicutes, in the family Haloanaerobiaceae, order Haloanaerobiales, and is the only member of this order whose genome has been completely sequenced. The availability of the genome sequence will not only enhance our understanding of survival and adaptation strategies of microbes living under dual extremities of high salt and t
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Books on the topic "Α-amylase"

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Mazur, Allan. Physiology of Face-to-Face Competition. Edited by Rosemary L. Hopcroft. Oxford University Press, 2018. http://dx.doi.org/10.1093/oxfordhb/9780190299323.013.24.

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Face-to-face competition for rank in human status hierarchies is similar to “dominance competition” in other primate species, particularly the African apes. Each individual has signs or signals showing that it has or ought to have high or low status. Group members may accept these signs at face value, or one individual may challenge another for high rank. Among apes and humans, such dominance contests are usually nonviolent, often taking the form of an exchange of stressful signals. Eventually, one contestant withdraws or concedes the higher rank, thus lowering the stress level. Serious compet
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Book chapters on the topic "Α-amylase"

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Makkar, Harinder P. S., P. Siddhuraju, and Klaus Becker. "α-Amylase Inhibitor." In Plant Secondary Metabolites. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-425-4_3.

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Schreckinger, Maria, Mary Ann Lila, Gad Yousef, and Elvira de Mejia. "Inhibition of α-Glucosidase and α-Amylase byVaccinium floribundumandAristotelia chilensisProanthocyanidins." In ACS Symposium Series. American Chemical Society, 2012. http://dx.doi.org/10.1021/bk-2012-1109.ch006.

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Berre, V. Anton-Le, C. Gilles, F. Payan, and P. Rougé. "Molecular Interaction of the α-Amylase Inhibitor from Phaseolus vulgaris Seeds with Pig Pancreatic α-Amylase." In Plant Proteins from European Crops. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03720-1_3.

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Butterworth, Peter J., and Peter R. Ellis. "Kinetics of α-Amylase Action on Starch." In Interdisciplinary Approaches to Food Digestion. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-03901-1_14.

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Ho, M. F., X. Yin, F. F. Filho, F. Lajolo, and J. R. Whitaker. "Naturally occurring α-amylase inhibitors: Structure/function relationships." In Protein Structure-Function Relationships in Foods. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2670-4_5.

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Whitaker, John R. "Protease and α-Amylase Inhibitors of Higher Plants." In ACS Symposium Series. American Chemical Society, 1997. http://dx.doi.org/10.1021/bk-1997-0662.ch002.

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Saha, Badal C., Saroj P. Mathupala, and J. Gregory Zeikus. "Comparison of Amylopullulanase to α-Amylase and Pullulanase." In ACS Symposium Series. American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch027.

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Martinez, Mario M., and Manuel Gómez. "Insight of the α-Amylase Family of Enzymes." In Microbial Enzyme Technology in Food Applications. CRC Press, 2017. http://dx.doi.org/10.1201/9781315368405-4.

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Chambliss, G. H., and W. L. Nicholson. "Regulation of α-Amylase Synthesis in Bacillus Subtilis." In Gene Manipulation and Expression. Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-011-6565-5_4.

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Carbonero, P., I. Díaz, J. Vicente-Carbajosa, J. Alfonso-Rubí, K. Gaddour, and P. Lara. "Cereal α-amylase/trypsin inhibitors and transgenic insect resistance." In Developments in Plant Breeding. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4475-9_17.

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Conference papers on the topic "Α-amylase"

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Dieguez-Santana, Karel, та Bakhtiyor Rasulev. "Machine Learning Analysis of α-amylase Inhibitors". У MOL2NET'21, Conference on Molecular, Biomedical & Computational Sciences and Engineering, 7th ed. MDPI, 2021. http://dx.doi.org/10.3390/mol2net-07-11229.

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Keke, Anete, та Ingmars Cinkmanis. "α-amylase activity in freeze-dried and spray-dried honey". У Research for Rural Development 2020. Latvia University of Life Sciences and Technologies, 2020. http://dx.doi.org/10.22616/rrd.26.2020.017.

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Honey is a naturally supersaturated sugar solution, which tends to crystallize. The crystallization of honey can lead to unwanted fermentation that can have a negative impact to honey quality. The production of honey powder could be an alternative method to prevent honey from fermentation. Honey powder could be used as alternative substitute to liquid honey that would allow to use this product more widely in the food industry. α-amylase activity is one of the most important parameters to evaluate the quality of honey. The aim of this study was to investigate the effect of freeze-drying and spr
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Shaik, Mahammad Sadik, Venkata Narasimha Reddy Kuduthuri, Anil Kumar Kusetty, Pavan Kumar Banaganipalli та Lakshmi Silpa Kandukuri. "Green synthesis of α-hydroxyphosphonates and assessment of their α-amylase activity in vitro". У THE 6TH INTERNATIONAL CONFERENCE OF ICE-ELINVO 2023: Digital Solutions for Sustainable and Green Development. AIP Publishing, 2025. https://doi.org/10.1063/5.0248022.

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JOSHI, VARSHA S., та B. N. THORAT. "OPTIMIZATION OF PROCESS PARAMETERS FOR SPRAY DRYING OF α-AMYLASE". У The Proceedings of the 5th Asia-Pacific Drying Conference. World Scientific Publishing Company, 2007. http://dx.doi.org/10.1142/9789812771957_0035.

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Saini, Nancy, Ritika Sirohi, Paranjeet Kaur, Pankaj Wadhwa, Neetu Saini та Sanjeev Kumar Sahu. "Role of phytoconstituents as natural α-amylase inhibitors: A review". У THE FOURTH SCIENTIFIC CONFERENCE FOR ELECTRICAL ENGINEERING TECHNIQUES RESEARCH (EETR2022). AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0168944.

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Primožič, Mateja, Željko Knez та Maja Leitgeb. "Activity of α--Amylase from P. ostreatus Grown on Waste Substrates". У International Conference on Technologies & Business Models for Circular Economy. University of Maribor Press, 2022. http://dx.doi.org/10.18690/um.fkkt.2.2022.7.

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Forest and agricultural waste can be a major development and ecological opportunity. Therefore, it is reasonable to use biological waste further to produce energy and for the manufacture of certain products with high added value, such as, for example, the cultivation of fungi and, consequently, the production of biocatalysts with high market value. In addition, the use of agriculture waste for Oyster mushroom (Pleurotus ostreatus) growth can be integrated to waste management and the development of the bioeconomy. The cultivation of P. ostreatus using waste plant biomass from agriculture (straw
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Ishartati, Erny, Dyah Roeswitawati, Sukardi, Saefur Rohman та Sudiadi. "α-Glucosidase and α -Amylase Inhibitory Activities of Jambolan (Syzygium cumini (L.) SKEELS) Fruit and Seed". У 3rd KOBI Congress, International and National Conferences (KOBICINC 2020). Atlantis Press, 2021. http://dx.doi.org/10.2991/absr.k.210621.043.

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Srećković, N., N. Mihailović та V. Mihailović. "Lysimachia vulgaris L. aerial part and root methanol extracts as potential α-amylase and α-glucosidase inhibitors". У GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1759175.

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Aijijiyah, Nur Pasca, Farah Mahzumi та Mardi Santoso. "α-Amylase inhibitory activity of (E)-N’-(3-(4-bromophenyl)acryloyl)isonicotinohydrazide". У THE FOURTH AL-NOOR INTERNATIONAL CONFERENCE FOR SCIENCE AND TECHNOLOGY (4NICST2022). AIP Publishing, 2024. http://dx.doi.org/10.1063/5.0205814.

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"Optimization of production conditions for α-amylase as an important biodesizing agent". У INTERNATIONAL CONFERENCE ON BIOLOGICAL RESEARCH AND APPLIED SCIENCE. Jinnah University for Women, 2024. http://dx.doi.org/10.37962/ibras/2024/79-80.

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Reports on the topic "Α-amylase"

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Karcheva-Bahchevanska, Diana, Paolina Lukova, Mariana Nikolova, Rumen Mladenov та Iliya Iliev. Inhibition Effect of Bulgarian Lingonberry (Vaccinium vitis-idaea L.) Extracts on α‒Amylase Activity. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2019. http://dx.doi.org/10.7546/crabs.2019.02.10.

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Farazi, Mena, Michael Houghton, Barbara Cardoso, Margaret Murray та Gary Williamson. A systematic review of the inhibitory effect of extracts from edible parts of nut on α-amylase activity. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, 2023. http://dx.doi.org/10.37766/inplasy2023.8.0030.

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Yibchok-anun, Sirinthorn, Wijit Banlunara, and Sirichai Adisakwattana. Antidiabetic effects, mechanisms of of p-methoxy-trans-cinnamic acid. Faculty of Veterinary Science, Chulalongkorn University, 2008. https://doi.org/10.58837/chula.res.2008.81.

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p-Methoxycinnamic acid (p-MCA) is a cinnamic acid derivative that shows various pharmacologic actions such as neuroprotective and hepatoprotective activities. To examine the insulinotropic activity of p-MCA, the perfused rat pancreas and a pancreatic β-cell line, INS-1 were used in the studies. P-MCA increased insulin secretion from the perfused rat pancreas and INS-1 cells in a concentration-dependent manner. In addition, p-MCA increased intracellular Ca²⁺ concentration ([Ca²⁺]i) in INS-1 cells. The p-MCA-induced insulin secretion and rise in [Ca²⁺]i were markedly inhibited in the absence of
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