DIVERSITY OF BIOCHEMICAL AND BIOPHYSICAL PROPERTIES OF THE GDSL LIPASE FAMILY
Lipolytic enzyme is an enzyme that catalyzes the ester bond hydrolysis on triacylglyceride. According to the length of the fatty acid chains that has been hydrolysed, lipolytic enyzme is categorized as lipase (EC 3.1.1.3) and as carboxylesterase (EC 3.1.1.1). Lipases are enzymes with functions in th...
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| Format: | Final Project |
| Language: | Indonesia |
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| Online Access: | https://digilib.itb.ac.id/gdl/view/55001 |
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| Institution: | Institut Teknologi Bandung |
| Language: | Indonesia |
| Summary: | Lipolytic enzyme is an enzyme that catalyzes the ester bond hydrolysis on triacylglyceride. According to the length of the fatty acid chains that has been hydrolysed, lipolytic enyzme is categorized as lipase (EC 3.1.1.3) and as carboxylesterase (EC 3.1.1.1). Lipases are enzymes with functions in the hydrolisis of triglycerides into glycerols and fatty acid. Moreover, the enyzme also has function in transesterification, alcoholysis, acidolysis, esterification, and aminolysis. The sources of lipases are from plants, animals and microorganisms. The most useful property of lipases is their substrate specification. GDSL lipase is a new sub-class of lipases that have a GDSL motif with the active site ser near the N-terminal. The unique structure of GDSL lipase makes it has an active site that is flexible to a variety choice of substrates. Bacillus aquimaris MKSC 6.2 from the sea surrounding Merak Kecil Island, Banten, West Java has been identified as having the gene coding for the lipolytic enzyme GDSL but the detailed characteristic of the enzyme has not been explored yet. The purpose of this study is to analyse the structure model of GDSL Lipase from Bacillus aquimaris MKSC
6.2 and to study homology analysis among the lipolytic enyzmes, and to review the biochemical and biophysical properties of lipolytic enzymes. To achieve the research objectives, the structure model was firstly searched with a help of HHPRED and BLAST, the protein model was constructed with Swiss Model as well as with the I-Tasser server. The research results show that the amino acid sequences of the GDSL lipase family are very diverse, although the conservation sequences of the N-terminal is very consistent with the GDSL motives. The GDSL lipase family also has a variety of structures and biochemical properties. |
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