Kekhususan Substrat Lipase Miselium Rhizopus oryzae
The substrate specificity of a mycelial lipase from Rhizopus oryzae for the esterification reaction was investigated. Studies showed that the enzyme exhibited high activity when long-chain fatty acids (Cl2-Cl8) were reacted with primary alcohols (C3-C7) as well as primary diols. The presence of dou...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English Malay |
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Universiti Putra Malaysia Press
1996
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| Online Access: | http://psasir.upm.edu.my/id/eprint/3232/ http://psasir.upm.edu.my/id/eprint/3232/1/Kekhususan_Substrat_Lipase_Miselium.pdf |
| _version_ | 1848839471911403520 |
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| author | Salleh, Abu Bakar Wan Yunus, Wan Md Zin Basri, Mahiran Ampon, Kamaruzaman Abdul Razak, Che Nyonya |
| author_facet | Salleh, Abu Bakar Wan Yunus, Wan Md Zin Basri, Mahiran Ampon, Kamaruzaman Abdul Razak, Che Nyonya |
| author_sort | Salleh, Abu Bakar |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | The substrate specificity of a mycelial lipase from Rhizopus oryzae for the esterification reaction was investigated. Studies showed that the enzyme exhibited high activity when long-chain fatty acids (Cl2-Cl8) were reacted with primary alcohols (C3-C7) as well as primary diols. The
presence of double bonds did not affect reactions significantly, but esterification activity for secondary, tertiary or aromatic alcohols was low. |
| first_indexed | 2025-11-15T07:11:59Z |
| format | Article |
| id | upm-3232 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English Malay |
| last_indexed | 2025-11-15T07:11:59Z |
| publishDate | 1996 |
| publisher | Universiti Putra Malaysia Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-32322013-05-27T07:06:37Z http://psasir.upm.edu.my/id/eprint/3232/ Kekhususan Substrat Lipase Miselium Rhizopus oryzae Salleh, Abu Bakar Wan Yunus, Wan Md Zin Basri, Mahiran Ampon, Kamaruzaman Abdul Razak, Che Nyonya The substrate specificity of a mycelial lipase from Rhizopus oryzae for the esterification reaction was investigated. Studies showed that the enzyme exhibited high activity when long-chain fatty acids (Cl2-Cl8) were reacted with primary alcohols (C3-C7) as well as primary diols. The presence of double bonds did not affect reactions significantly, but esterification activity for secondary, tertiary or aromatic alcohols was low. Universiti Putra Malaysia Press 1996 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/3232/1/Kekhususan_Substrat_Lipase_Miselium.pdf Salleh, Abu Bakar and Wan Yunus, Wan Md Zin and Basri, Mahiran and Ampon, Kamaruzaman and Abdul Razak, Che Nyonya (1996) Kekhususan Substrat Lipase Miselium Rhizopus oryzae. Pertanika Journal of Science & Technology, 4 (1). pp. 23-29. ISSN 0128-7680 Malay |
| spellingShingle | Salleh, Abu Bakar Wan Yunus, Wan Md Zin Basri, Mahiran Ampon, Kamaruzaman Abdul Razak, Che Nyonya Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title | Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title_full | Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title_fullStr | Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title_full_unstemmed | Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title_short | Kekhususan Substrat Lipase Miselium Rhizopus oryzae |
| title_sort | kekhususan substrat lipase miselium rhizopus oryzae |
| url | http://psasir.upm.edu.my/id/eprint/3232/ http://psasir.upm.edu.my/id/eprint/3232/1/Kekhususan_Substrat_Lipase_Miselium.pdf |