Thermoalkalophilic lipase from an extremely halophilic bacterial strain Bacillus atrophaeus FSHM2: Purification, biochemical characterization and application-Reference-Cited by-同舟云学术

Thermoalkalophilic lipase from an extremely halophilic bacterial strain Bacillus atrophaeus FSHM2: Purification, biochemical characterization and application

Published:2017-04-18 Issue:3 Volume:35 Page:151-160
ISSN:1024-2422
Container-title:Biocatalysis and Biotransformation
language:en
Short-container-title:Biocatalysis and Biotransformation

Author:

Ameri Atefeh¹,Shakibaie Mojtaba¹,Faramarzi Mohammad Ali²,Ameri Alieh³,Amirpour-Rostami Sahar¹,Rahimi Hamid Reza⁴,Forootanfar Hamid⁵

Affiliation:

1. Pharmaceutics Research Center, Institute of Neuropharmacology, Kerman University of Medical Sciences, Kerman, Iran;

2. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran;

3. Department of Medicinal Chemistry, Faculty of Pharmacy, Kerman University of Medical Sciences, Kerman, Iran;

4. Department of Toxicology and Pharmacology, Faculty of Pharmacy, Kerman University of Medical Sciences, Kerman, Iran;

5. Herbal and Traditional Medicines Research Center, Kerman University of Medical Sciences, Kerman, Iran

Funder

Kerman University of Medical Sciences

Herbal and Traditional Medicines Research Center, Kerman University of Medical Sciences, Kerman, Iran

Publisher

Informa UK Limited

Subject

Biochemistry,Catalysis,Biotechnology

Link

https://www.tandfonline.com/doi/pdf/10.1080/10242422.2017.1308494

Reference38 articles.

1. Metal ion activated lipase from halotolerant Bacillus sp. VITL8 displays broader operational range

2. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

3. Purification and characterization of an organic solvent-stable lipase from Pseudomonas stutzeri LC2-8 and its application for efficient resolution of (R, S)-1-phenylethanol

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