Characterisation of Amylase Activity in Selected Aspergillus Species
Enzymes are biological catalysts that have several remarkable properties. They played an important role throughout the development of the human race where they have been used in industries since the 19th century. Amylase which hydrolyse starch is a member of the group hydrolase, where it is an impo...
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Format: | Final Year Project Report |
Language: | English English |
Published: |
Universiti Malaysia Sarawak, (UNIMAS)
2022
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Online Access: | http://ir.unimas.my/id/eprint/39824/1/KAREN%20HON%20JING%20YI%2024pgs.pdf http://ir.unimas.my/id/eprint/39824/4/KAREN%20HON%20JING%20YI%20ft.pdf http://ir.unimas.my/id/eprint/39824/ |
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Institution: | Universiti Malaysia Sarawak |
Language: | English English |
Summary: | Enzymes are biological catalysts that have several remarkable properties. They played an important role
throughout the development of the human race where they have been used in industries since the 19th century. Amylase which hydrolyse starch is a member of the group hydrolase, where it is an important enzyme in the industry that occupies a third of the industrial enzyme production around the world. Most industrial enzymes are obtained from fungi and yeasts, where members of Aspergillus genus are producing a significant amount of amylase. However, production of amylase by three selected Aspergillus species which
are A. fumigatus, A. niger and A. sydowii after a long preservation period remains unknown, where it is also
of interest to compare amylase production of these fungi. The solid-based method was applied to screen for
amylase production and amylase production of the three species was studied through evaluating the Enzymatic Activity Index (EAI). The production of amylase from the three fungi species was confirmed as there are formation of halo zones. Amylase production was found to differ significantly among the three species, where A. sydowii exhibited the highest average EAI of 1.1027 ± 0.0228, followed by A. fumigatus (0.9056 ± 0.0105) and A. niger (0.8515 ± 0.0237). |
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