Isolation and screening of pectinase producing thermotolerant fungi
Pectin is a substance that has a very complex macromolecule and it can be found abundantly in the primary cell wall of the plants. Enzyme that helps to break down this polysaccharide substrate is known as pectinase enzyme and it catalyzes the pectin degradation through de-esterification and depolyme...
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| Main Author: | |
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| Format: | Project Paper Report |
| Language: | English |
| Published: |
2015
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| Online Access: | http://psasir.upm.edu.my/id/eprint/91022/1/FBSB%202015%20134%20-%20IR.pdf http://psasir.upm.edu.my/id/eprint/91022/ |
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| Institution: | Universiti Putra Malaysia |
| Language: | English |
| Summary: | Pectin is a substance that has a very complex macromolecule and it can be found abundantly in the primary cell wall of the plants. Enzyme that helps to break down this polysaccharide substrate is known as pectinase enzyme and it catalyzes the pectin degradation through de-esterification and depolymerisation reactions. One of the current challenges in agricultural and fruit juice processing industries is the increasing of pollution problems due to the abundant amount of organic waste materials from agricultural and fruit juice processing industries. Besides that, there is also extensive demands of pectinase production for the extraction and clarification of fruit juices industry. Therefore, potential fungi with a high pectinolytic activity as well as its thermostability should be isolated and discovered so that they can be exploited for the degradation of organic waste materials in environment and their potential applications in the industry can be explored. This pectinase enzyme can be synthesized by thermotolerant fungi isolated from watery soil. This research study is designed to explore the potential of other strains of thermotolerant fungi that can produce pectinase and to study their pectinolytic activity. Comparison of the pectinolytic activity between thermotolerant fungi was done by studying the pectinolytic activity of each thermotolerant fungus. The polygalacturonase activity for isolates CP1 and CP2 were 1.3129 Uml-1 and 0.8856 Uml-1 respectively. The specific enzyme activity for CP1 is 23.5587 Umg-1 while for CP2 is 21.7635 Umg-1. Isolate CP1 was found to have a higher enzyme activity in polygalacturonase enzyme activity. For the identification of thermotolerant fungi, both isolates were identified as Aspergillus fumigatus but from different strains. |
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