Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions-Reference-Cited by-同舟云学术

Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions

Published:2022-10-17 Issue: Volume: Page:
ISSN:2149-6366
Container-title:Türk Doğa ve Fen Dergisi
language:tr
Short-container-title:TDFD

Author:

COLAK Dilsat Nigar¹

Affiliation:

1. Giresun Üniversitesi

Abstract

A novel amylase producing bacterium FAD4 was isolated from the wastewater of a textile factory located in Soke (Aydın/Turkey). The amylase production ability of gram positive, coccoidal FAD4 strain was confirmed with plate assay. Morphological and 16S rRNA sequence analyses revealed that FAD4 belongs to the Brachybacterium paraconglomeratum species with a sequence similarity of 99.8%. The optimal conditions for amylase production were determined as 72 h at 30 °C with supplementation of 1% starch. Optimum temperature and pH of the amylase were 50 °C and 7.0 respectively. Different starch, carbon and nitrogen sources were investigated for amylase production. A high enzyme production was observed with 1% potato starch and among nitrogen sources peptone was induced the production of amylase. Lactose, galactose, and fructose were also increased the enzyme production as carbon sources.

Publisher

Bingol Universitesi

Subject

General Earth and Planetary Sciences,General Environmental Science

Reference32 articles.

1. [1] Li S, Yang X, Yang S, Zhu M, Wang X. Technology prospecting on enzymes: application, marketing and engineering. Comput. Struct. Biotechnol. J. 2012;2:1–11.

2. [2] Gomes I, Gomes J, Steiner W. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresour. Technol. 2003;90 (2);207-214.

3. [3] Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37;233–238.

4. [4] Nagano N, Orengo C.A, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 2002;321;741-765.

5. [5] Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial α-amylases: a biotechnological perspective. Process Biochem. 2003;38;1599 – 1616.