Phenolase in Norway lobster (Nephrops norvegicus): activation and purification

Yan, Xinjian and Taylor, K. D. Anthony and Hanson, Steven W. (1990) Phenolase in Norway lobster (Nephrops norvegicus): activation and purification. Food Chemistry, 36 (1). pp. 19-30. ISSN 0308-8146

Full content URL: http://dx.doi.org/10.1016/0308-8146(90)90004-N

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Item Type:Article
Item Status:Live Archive

Abstract

Increase in phenolase activity from Norway lobster was observed to take place immediately after making a crude enzyme preparation; the total enzyme activity increased by a factor of 3–4 over a period of 8–12 h. The process was associated with the appearance of a more active form of the phenolase. The initial natural form (Form I) and the more active form (Form II) of the enzyme were separated and partially purified by a combination of acetone precipitation and DEAE cellulose column chromatography. The natural form (Form I) was found to have an optimum temperature of 40°C, an isoelectric point of 4·7, a molecular weight of 667 000 and a Km towards catechol of 21·8 mm, whereas the more active form (Form II) was found to have an optimum temperature of 45°C, an isoelectric point of 6·1, a molecular weight of 141 000, and a Km towards catechol of 2·84 mm.

Keywords:Phenolase, Lobster
Subjects:D Veterinary Sciences, Agriculture and related subjects > D610 Food Science
Divisions:College of Science > National Centre for Food Manufacturing
ID Code:9548
Deposited On:20 May 2013 11:03

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