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Purification and properties of two pectinesterases from tomatoes
1Richard B. Russell Agricultural Research Center, US Department of Agriculture, Agricultural Research Service, Athens, GA 30613.
Phytochemistry
|April 1, 1992
Summary
Pectinesterase levels rise during tomato ripening. Researchers purified and characterized two major pectinesterase isoenzymes, finding differences but also similarities in their structure and antibody cross-reactivity.
Area of Science:
- Plant Biochemistry
- Fruit Ripening Studies
- Enzymology
Background:
- Pectinesterase (PE) is a key enzyme in fruit ripening, particularly in tomatoes.
- While several PE isoenzymes exist in tomatoes, one typically dominates most cultivars.
- Unique PE profiles have been observed in certain cherry tomato varieties.
Purpose of the Study:
- To investigate the distinct pectinesterase isoenzymes found in specific tomato cultivars.
- To purify and characterize the major pectinesterase isoenzymes from tomato fruit.
- To compare the biochemical and structural properties of these purified pectinesterases.
Main Methods:
- Enzyme purification to homogeneity.
- Biochemical characterization of purified enzymes.
- Immunological assays (antibody cross-reactivity).
- N-terminal amino acid sequencing.
Main Results:
- Two major pectinesterase isoenzymes were successfully purified from tomato fruit.
- Significant biochemical differences were identified between the two isoenzymes.
- Both isoenzymes exhibited cross-reactivity with specific antibodies.
- N-terminal amino acid sequences showed notable similarity.
Conclusions:
- Tomato fruit contain distinct pectinesterase isoenzymes with varying characteristics.
- Despite differences, structural similarities exist, as indicated by antibody cross-reactivity and sequence data.
- Further research into these isoenzymes could elucidate their specific roles in tomato ripening and quality.