Plant and algal interference in bacterial beta-D-galactosidase and beta-D-glucuronidase assays.

Appl Environ Microbiol

Centre for Advanced Analytical Chemistry, CSIRO Division of Coal and Energy Technology, Menai, New South Wales, Australia.

Published: November 1994

Several commonly occurring freshwater and marine plants and algae were screened for beta-D-galactosidase and beta-D-glucuronidase activities by using a 60-min enzyme assay based on the hydrolysis by these enzymes of 4-methylumbelliferyl-beta-D-galactoside and 4-methylumbelliferyl- beta-glucuronide, respectively. All freshwater plant extracts tested showed beta-D-galactosidase activity several at relatively high levels, and a number also showed beta-D-glucuronidase activity. A number of the macroalgae showed no activity of either enzyme, but those showing beta-D-galactosidase activity also showed beta-D-glucuronidase activity. The majority of microalgae showed some beta-D-galactosidase activity, but few showed beta-D-glucuronidase activity. Further studies, using the commercial Colilert test and the marine water formulation of Colilert, revealed that 2 of 11 of the microalgal species and several of the plant extracts tested caused positive reactions. It was concluded that several plant extracts and algae could significantly interfere with the detection of coliform bacteria and Escherichia coli with the use of rapid assays, on the basis of their production of beta-D-galactosidase and beta-D-glucuronidase, respectively. The significance of the plant and algal interferences in tests such as Colilert is dependent on the levels of enzymes released under natural conditions, the dilution which they may undergo, and the numbers of algal cells present. This also applies to interferences in rapid enzyme assays.(ABSTRACT TRUNCATED AT 250 WORDS)

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC201922PMC
http://dx.doi.org/10.1128/aem.60.11.3959-3964.1994DOI Listing

Publication Analysis

Top Keywords

beta-d-galactosidase beta-d-glucuronidase
12
plant extracts
12
beta-d-galactosidase activity
12
beta-d-glucuronidase activity
12
plant algal
8
extracts tested
8
activity beta-d-glucuronidase
8
activity
7
beta-d-galactosidase
6
beta-d-glucuronidase
6

Similar Publications

Increasing crop productivity in an ever-changing environmental scenario is a major challenge for maintaining the food supply worldwide. Generation of crops having broad-spectrum pathogen resistance with the ability to cope with water scarcity is the only solution to feed the expanding world population. Stomatal closure has implications on pathogen colonization and drought tolerance.

View Article and Find Full Text PDF

Purpose: Adaptation of the colorimetric method for the determination of β-d-galactosidase, β-d-glucuronidase and α-l-fucosidase activities in serums from hemolyzed blood, the material currently being discarded.

Materials And Methods: The materials included serums from hemolyzed and non-hemolyzed blood, obtained from 26 healthy volunteers. The adaptation of the method involved precipitation of the proteins with trichloroacetic acid after incubating serums with substrates, but before determining the products of enzymatic reactions.

View Article and Find Full Text PDF

Objective: To elucidate the key biochemical indexes associated with 1, 2-dimethylhydrazine (DMH)-induced colon carcinogenesis and the modulatory efficacy of a dietary polyphenol, ellagic acid (EA).

Materials And Methods: Wistar rats were chosen to study objective, and were divided into 4 groups; Group 1-control rats; Group 2-rats received EA (60 mg/kg body weight/day, orally); rats in Group 3-induced with DMH (20 mg/kg body weight) subcutaneously for 15 weeks; DMH-induced Group 4 rats were initiated with EA treatment. We examined key citric acid cycle enzymes such as isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase and the activities of respiratory chain enzymes NADH dehydrogenase and Cytochrome-C-oxidase and membrane-bound enzyme profiles (Na +/K + ATPase, Ca 2+ ATPase and Mg 2+ ATPase), activities of lysosomal proteases such as β-D-glucuronidase, β-galactosidase and N-acety-β-D-glucosaminidase and cellular thiols (oxidized glutathione, protein thiols, and total thiols).

View Article and Find Full Text PDF

A sensitive and robust method for automated on-line monitoring of enzymatic activities in water and water resources.

Water Sci Technol

May 2014

Institute of Chemical Engineering, Research Group Environmental Microbiology and Molecular Ecology, Vienna University of Technology, Gumpendorferstraße 1A/166-5-2, A-1060 Vienna, Austria E-mail: Vienna University of Technology, Interuniversity Cooperation Centre for Water and Health, Gumpendorferstraße 1a, 1060 Vienna, Austria.

The realisation of a novel concept for automated on-line monitoring of enzymatic activities in water was successfully demonstrated by long-term field testing at two remote Austrian ground water resources. The β-D-glucuronidase (GLUC) activity was selected as a representative enzymatic model parameter for the on-line determination. But the device can be adapted for any enzymatic reaction with diagnostic relevance for microbial water quality monitoring, as demonstrated for the β-D-galactosidase activity.

View Article and Find Full Text PDF

Fast detection and quantification of Escherichia coli using the base principle of the microbial fuel cell.

J Environ Manage

November 2013

Department of Civil and Environmental Engineering, KAIST, Daejeon 305-701, Republic of Korea.

Escherichia coli is an important microbial indicator of fecal contamination, making accurate quantitative detection of E. coli a key to ensuring public health. In this study, a microbial fuel cell (MFC) was used as a detection unit of an E.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!