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Akio Sugihara
Researcher at Tokushima Bunri University
Publications - 107
Citations - 5258
Akio Sugihara is an academic researcher from Tokushima Bunri University. The author has contributed to research in topics: Lipase & Triacylglycerol lipase. The author has an hindex of 38, co-authored 107 publications receiving 5132 citations.
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Journal ArticleDOI
Amino acid sequence of thermostable direct hemolysin produced by Vibrio parahaemolyticus.
Susumu Tsunasawa,Akio Sugihara,Takeharu Masaki,Fumio Sakiyama,Yoshifumi Takeda,Toshio Miwatani,Kozo Narita +6 more
TL;DR: The primary structure of hemolysin elucidated in the present study is essentially the same as that deduced from the nucleotide sequence of a gene encoding the protein but differs in 9 amino acid residues, suggesting the possibility of the presence of multiple genes for the thermostable direct hemoly sin in Vibrio parahaemolyticus.
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Stepwise ethanolysis of tuna oil using immobilized Candida antarctica lipase.
TL;DR: The two- and three-step ethanolyses achieved the conversion of 95% or more of tuna oil to its corresponding E-FAs and the lipase stability was investigated by transferring the enzyme to a fresh substrate mixture of the first step after finishing one cycle of reaction.
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Cloning, Nucleotide Sequencing, and Expression in Escherichia coli of a Lipase and Its Activator Genes from Pseudomonas sp. KWI-56
TL;DR: A lipase gene (lip) and its activator gene (act) on a 2.9 kb BglII-EcoRI fragment from Pseudomonas sp.
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Production of structured lipids containing essential fatty acids by immobilizedRhizopus delemar lipase
Yuji Shimada,Akio Sugihara,Hirofumi Nakano,Tomomi Yokota,Toshihiro Nagao,Sadao Komemushi,Yoshio Tominaga +6 more
TL;DR: In this paper, an attempt was made to produce structured lipids containing essential fatty acid by acidolysis with 1,3positional specificRhizopus delemar lipase.
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Cloning and Nucleotide Sequence of cDNA Encoding a Lipase from Fusarium heterosporum
TL;DR: A 1.3-kbp lipase cDNA was isolated from the cDNA library by colony hybridization with an oligonucleotide probe corresponding to the N-terminal amino acid sequence, and it was suggested that the catalytic triad was composed of Ser144, Asp198, and His256.