Thermophilic laccase from xerophyte species Opuntia vulgaris.
Summary of "Thermophilic laccase from xerophyte species Opuntia vulgaris."
Two laccase temperature isoforms capable of oxidizing phenolic compounds to quinones were isolated and purified to homogeneity from the cladodes of the xerophyte species Opuntia vulgaris. These catalytically active proteins exhibit apparent molecular masses of 137 and 90 kDa. Under reducing conditions, both isoforms yielded a subunit molecular mass of 43 kDa, suggesting that the enzyme is a multimer of the 43 kDa subunit. The 137 kDa isoform when heated at 80 degrees C for 3min generated three polypeptide bands on activity stained polyacrylamide gels exhibiting 137, 90 and 43 kDa molecular forms. All isoforms of the enzyme exhibited an optimum pH of 10 when 2,6-dimethoxyphenol was used as a substrate. The optimum temperature of the 137 kDa enzyme form was noted to be 80 degrees C and that of the 90 kDa enzyme form was 70 degrees C. Denaturation kinetics of both the laccase isoforms carried out at their respective optimum temperatures for 30 min exhibited enzyme activity in excess of their t(1/2) values throughout the assay period. The K(m) for the 137 kDa form was determined to be 2.2 +/- 0.3 mm and the V(max) was 2.8 +/- 0.2 IU/mL. These high temperature stable laccase isoforms having alkaline pH optima can find significant industrial use. Copyright (c) 2010 John Wiley & Sons, Ltd.
Department of Biochemistry and Molecular Biology, School of Life Sciences, Pondicherry University, Puducherry 605014, India.
This article was published in the following journal.
Name: Biomedical chromatography : BMC
The essential oils from the cladodes of Opuntia littoralis, Opuntia ficus-indica and Opuntia prolifera growing wild on Santa Catalina Island, California, were obtained by hydrodistillation and analyse...
The ERY4 laccase gene from Pleurotus eryngii was expressed in Saccharomyces cerevisiae and the recombinant laccase resulted to be not biologically active. This gene was thus modified to obtain chimeri...
High cost becomes the major obstacle for the industrial application of laccase. Many approaches have been applied to enhance the yield and decrease the cost of laccase. Since flavonoids are the natura...
Laccase (EC 220.127.116.11) activity was measured in regenerating and non-regenerating protoplasts isolated from tobacco (Nicotiana tabacum, L.) leaves. Laccase activity diminished soon after isolation: the...
The use of ionic liquids (ILs) as reaction media for enzymatic reactions has increased its potential because they can improve enzyme activity and stability. Kinetic and stability properties of immobil...
The purpose of this study is to assess the effectiveness of IDP-110 in treating patients with acne vulgaris.
The purpose of this study is to determine whether KC706 is effective in the prevention and healing of blisters in patients with pemphigus vulgaris, while the patient remains on stable dose...
The purpose of this study is to assess the safety and effectiveness of IDP-107 in treating patients with acne vulgaris.
The purpose of the study is to find out about the effectiveness and the safety of an investigational drug called etanercept (Enbrel) to treat pemphigus vulgaris. Pemphigus vulgaris is a po...
Patients with vitiligo vulgaris are treated with Pimecrolimus twice a day during 6 months. After a baseline visit, patient returns for a control visit after 3 and 6 months of treatment. On...
Medical and Biotech [MESH] Definitions
A plant genus of the family CACTACEAE. Species with cylindrical joints are called Cholla; flat jointed ones are Prickly-pear.
A species of gram-negative bacteria and nitrogen innoculant of PHASEOLUS VULGARIS.
A species of green microalgae in the family Chlorellaceae. It is used as a model organism for PHOTOSYNTHESIS, and as a food supplement (DIETARY SUPPLEMENTS).
A species of thermophilic CAMPYLOBACTER found in healthy seagulls and causing ENTERITIS in humans.
A species of the Beta genus. Cultivars are used as a source of beets (root) or chard (leaves).