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Decolorization method of crude alkaline protease preparation produced from an alkalophilic Bacillus clausii

Content Provider	Springer Nature Link
Author	Koo, Kwang Bon Joo, Han Seung Choi, Jang Won
Copyright Year	2011
Abstract	Diaion HPA75 decolorized efficiently the crude preparation of novel alkaline protease produced by Bacillus clausii. The optimum concentrations of HPA75 and contact time for efficient decolorization were determined to be approximately 6 ∼ 10% (w/v) and 8 h, respectively. Color removal efficiency was improved at alkaline pH, and 21% color intensity was retained with a protease yield of 99.7% at pH 11. By using highly concentrated samples, a pattern of decolorization was achieved that was similar to that produced by unconcentrated enzyme preparations. After treatment with 6% HPA75 for 8 h, the residual color intensity was approximately 20% with a protease yield of nearly 100%. Used HPA75 could be regenerated easily, and the regenerated HPA75 was as effective as the fresh HPA75 for decolorization and protease recovery. The regeneration efficiency of the used Diaion HPA75 was greater than 90% until it was used four times. Considering these results, we suggest Diaion HPA75 is suitable for color removal applications, producing high protease yields from fermented broth.
Starting Page	89
Ending Page	96
Page Count	8
File Format	PDF
ISSN	12268372
Journal	Biotechnology and Bioprocess Engineering
Volume Number	16
Issue Number	1
e-ISSN	19763816
Language	English
Publisher	The Korean Society for Biotechnology and Bioengineering
Publisher Date	2011-04-13
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	alkaline protease Bacillus clausii decolorization diaion HPA75 Biotechnology Industrial and Production Engineering
Content Type	Text
Resource Type	Article
Subject	Bioengineering Biomedical Engineering Applied Microbiology and Biotechnology Biotechnology

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