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Amylolytic enzymes of Lipomyces starkeyi: Purification and size-determination

Bignell, G.R., Bruce, Ian J., Evans, I.H. (2000) Amylolytic enzymes of Lipomyces starkeyi: Purification and size-determination. Biotechnology Letters, 22 (21). pp. 1713-1718. ISSN 0141-5492. (doi:10.1023/A:1005692300345) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:71969)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1023/A:1005692300345

Abstract

?-Amylase accumulated in the growth medium of the yeast Lipomyces starkeyi (NCYC 1436) to a maximum of 12 units ml-1 after 15 days' batch culture in a soluble starch medium. Extra ?-amylase activity, about 50 of that released into the medium, could be extracted from the cells by a salt wash. ?-Amylase was purified by salt precipitation followed by ion exchange chromatography and gel filtration. Native gel electrophoretic analysis showed the presence of three distinct amylolytic enzymes, with molecular weights of approximately 50, 70 and 80 kDa.

Item Type: Article
DOI/Identification number: 10.1023/A:1005692300345
Uncontrolled keywords: amylase, article; bacterium culture; electrophoresis; enzyme activity; enzyme purification; enzyme release; extraction; ion exchange chromatography; solubility; yeast, Bacteria (microorganisms); Lipomyces; Lipomyces starkeyi
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Sciences > School of Physical Sciences
Faculties > Sciences > School of Physical Sciences > Functional Materials Group
Depositing User: Ian Bruce
Date Deposited: 01 Feb 2019 12:55 UTC
Last Modified: 30 May 2019 08:49 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/71969 (The current URI for this page, for reference purposes)
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