Autor: |
Joel, Anaegbu Chinonso, Ayodeji, Orukotan Abimbola, Datsugwa, Mohammed Sani Sambo |
Předmět: |
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Zdroj: |
Annals: Food Science & Technology; 2018, Vol. 19 Issue 3, p551-557, 7p |
Abstrakt: |
Amylases are enzymes that break down starch or glycogen. The production of economically important alpha-amylases essential for the conversion of starches in oligosaccharides. The optimum condition for growth of Lysinibacillus xylanilyticus was best observed in Nutrient broth. The optimum pH range was found to be 6-10 and optimum temperature for growth was Phylogenetic analysis based on 16S rRNA gene sequences indicated that Lysinibacillus xylanilyticus ILBB210 16S ribosomal RNA gene, with accession number KT340486.1 was isolated from the soil and used for the production of amylase enzyme, while Molecular characterization and identification of fungi by internal transcribing sequence (ITS) sequencing. Lysinibacillus xylanilyticus showed abilities to produce amylase enzyme using nutrient starch agar during primary screening. The results revealed the abilities of lysinibacillus xylanilyticus and Lactobacillus acidophilus to ferment all sugars. While Lactobacillus brevis and Staphylococcus aureus only fermented sucrose and glucose and finally Lactobacillus plantarum only fermented sucrose. the screening of amylase activities of Bacillus sp in which bacteria isolate S3 had the highest enzyme activity of 0.542 compared to S1, S2, S4, S5 and S6 which had enzyme activity of 0.244, 0.122, 0.134, 0.187 and 0.161 respectively. Microorganisms of the Bacillus genus synthesise alpha amylase, and thus have the potential to dominate the enzyme industry. Bacillus sp are heterogeneous and are very versatile in their adaptability to environment. Various factors influence the nature of their metabolic process and the enzymes produced the result furthermore gives hope for a pharmaceutical composition wherein bonding amylase with another one auxillary material will be a good option to treat digestive disorders. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
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