<mods:mods version="3.0" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-0.xsd" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:mods="http://www.loc.gov/mods/v3"><mods:titleInfo><mods:title>Cloning of a Partial β-glucosidase Gene From Aspergillus terreus SUK-1</mods:title></mods:titleInfo><mods:name type="personal"><mods:namePart type="given"> </mods:namePart><mods:namePart type="family">Nik Marzuki Sidik</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given"> </mods:namePart><mods:namePart type="family">Shaiful Adzni Sharifuddin</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given"> </mods:namePart><mods:namePart type="family">Sahidan Senafi</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:abstract>The breakdown of cellulose to glucose is catalysed by a complex cellulase enzyme which is comprised of three classes of enzymes; endoglucanase, exoglucanase and β-glucosidase. Many studies have been done on cellulase and several genes encoding for β-glucosidase have been reported. Here we describe the cloning and sequence analysis of partial putative β-glucosidase gene from Aspergillus terreus SUK-1. Its potential to produce cellulase enzyme has been studied and reported. A pair of specific primer was designed from the conserved regions of several fungal sequences taken out from the GenBank. PCR amplification has successfully amplified a DNA fragment of approximately 233 bp and this fragment was cloned (designated as SA3). The sequence analysis with BLAST showed high similarity towards β-glucosidase gene and protein. 80% and 79% homology were observed between SA3 nucleotide sequence and β-glucosidase gene of A. niger and both A. kawachii and A. aculeatus. Whereas, amino acid sequence of SA3 showed 83% homology towards β-glucosidase of A. niger, A. kawachii and A. aculeatus.</mods:abstract><mods:classification authority="lcc">Q Science, Computer Science</mods:classification><mods:classification authority="lcc">R Medicine, Dentistry, Pharmacy, Nursing</mods:classification><mods:originInfo><mods:dateIssued encoding="iso8061">2005</mods:dateIssued></mods:originInfo><mods:originInfo><mods:publisher>Malaysian Society for Biochemistry and Molecular Biology</mods:publisher></mods:originInfo><mods:genre>Journal</mods:genre></mods:mods>