Isolation, expression, and characterization of raw starch degrading α-amylase from a marine lake Bacillus megaterium NL3
| Autor: | Dewi Yuliani, Nurul Widya, Dessy Natalia, Sofi Siti Shofiyah, Fernita Puspasari, Fean D. Sarian, Ihsanawati, Ocky Karna Radjasa |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Marine microorganism Starch medicine.disease_cause 03 medical and health sciences chemistry.chemical_compound Hydrolysis 0302 clinical medicine medicine Glycoside hydrolase Food science Amylase lcsh:Social sciences (General) lcsh:Science (General) Escherichia coli Bacillus megaterium Multidisciplinary Bacillus megaterium NL3 biology Canna food and beverages biology.organism_classification α-amylase 030104 developmental biology chemistry biology.protein lcsh:H1-99 Raw starch degrading enzyme 030217 neurology & neurosurgery Bacteria Research Article lcsh:Q1-390 |
| Zdroj: | Heliyon, Vol 6, Iss 12, Pp e05796-(2020) Heliyon |
| ISSN: | 2405-8440 |
| Popis: | A land-locked marine lake Kakaban with its significant ecological paramaters provides a unique habitat for bacteria with novel biotechnology potential that uses a diverse array of catalytic agents, including α-amylase. Aiming at the isolation of raw starch degrading α-amylase from marine biodiversity, a gene encoding BmaN2 from a sea anemone associated bacterium Bacillus megaterium NL3 was cloned and expressed in Escherichia coli ArcticExpress (DE3). It comprises an open reading frame of 1,563 nucleotides encoding BmaN2 of 520 amino acids and belongs to the glycoside hydrolase family 13 subfamily 36 (GH13_36). This α-amylase has a maximum activity at pH 6.0 and 60 °C with a specific activity of 28.7 U mg−1. The BmaN2 activity is enhanced strongly by Ca2+ but inhibited by EDTA. BmaN2 also exhibits high catalytic efficiency on soluble starch with kcat/KM value of 14.1 mL mg−1 s−1. Despite no additional starch-binding domain, BmaN2 is able to hydrolyze various raw starches, such as wheat, corn, cassava, potato, rice, sago, and canna, in which granular wheat is the preferred substrate for BmaN2. These characteristics indicate that BmaN2 is a promising raw starch degrading enzyme within the subfamily GH13_36. α-amylase, Bacillus megaterium NL3, marine microorganism, raw starch degrading enzyme |
| Databáze: | OpenAIRE |
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