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Toshiaki Osawa - One of the best experts on this subject based on the ideXlab platform.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin
2016Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-bindlng Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind a mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose. Lectins are carbohydrate-binding proteins and are particu-larly abundant in the seeds of leguminous plants (1, 2). Although the various legume lectins have different carbo-hydrate specificities, a high homology was found among the amino acid sequences of these lectins (3-16). The Bauhinia purpurea lectin (BPA) is specific for galactose and lactose, and binds Galy31-3GalNAc preferentially (17). We have already determined the complete amino acid sequence of BPA by means of cDNA cloning (8). To elucidate the correlation between the amino aci
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A chimeric lectin formed from Bauhinia purpurea lectin and Lens culinaris lectin recognizes a unique carbohydrate structure.
Journal of biochemistry, 2000Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Lectins are carbohydrate-binding proteins widely used in biochemical, immunochemical, and histochemical studies. Bauhinia purpurea lectin (BPA) is a leguminous lectin with an affinity for galactose and lactose. Nine amino acids, DTWPNTEWS, corresponding to the amino acid sequence from aspartic acid-135 to serine-143 in the primary structure of BPA were replaced with the corresponding amino acid residues from the mannose-binding Lens culinaris lectin (LCA), and the chimeric lectin obtained was expressed in Escherichia coli cells. The carbohydrate-binding specificity of the recombinant chimeric lectin was investigated in detail by comparing the elution profiles of various glycopeptides and oligosaccharides with defined carbohydate structures from immobilized lectin columns. Glycopeptides carrying three constitutive carbohydrate sequences of Galbeta1-3GalNAc-Ser/Thr and a complex-type biantennary glycopeptide, which show a high affinity for BPA or LCA, were shown to have no affinity for the chimeric lectin. In contrast, hybrid-type and high mannose-type glycopeptides with a Manalpha1-6(Manalpha1-3)Manalpha1-6Man sequence were found to have a moderate affinity for the chimeric lectin. This result demonstrates that a novel type of lectin with a unique carbohydrate-binding specificity can be constructed from BPA by substituting several amino acid residues in its metal-binding region with other amino acid residues. Additional lectin(s) with distinctly different carbohydrate-binding specificities will provide a powerful tool for many studies.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Abstract To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a d -galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose—Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the α- d -mannose binding Lens culinaris lectins. Although BPA is specific for β- d -galactose, the chimeric lectin expressed in Escherichia coli was found to bind α- d -mannosyl—bovine serum albumin and this binding was inhibited by d -mannose.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the alpha-D-mannose binding Lens culinaris lectins. Although BPA is specific for beta-D-galactose, the chimeric lectin expressed in Escherichia coli was found to bind alpha-D-mannosyl-bovine serum albumin and this binding was inhibited by D-mannose.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.
Journal of biochemistry, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind alpha mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose.
Kazuo Yamamoto - One of the best experts on this subject based on the ideXlab platform.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin
2016Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-bindlng Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind a mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose. Lectins are carbohydrate-binding proteins and are particu-larly abundant in the seeds of leguminous plants (1, 2). Although the various legume lectins have different carbo-hydrate specificities, a high homology was found among the amino acid sequences of these lectins (3-16). The Bauhinia purpurea lectin (BPA) is specific for galactose and lactose, and binds Galy31-3GalNAc preferentially (17). We have already determined the complete amino acid sequence of BPA by means of cDNA cloning (8). To elucidate the correlation between the amino aci
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A chimeric lectin formed from Bauhinia purpurea lectin and Lens culinaris lectin recognizes a unique carbohydrate structure.
Journal of biochemistry, 2000Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Lectins are carbohydrate-binding proteins widely used in biochemical, immunochemical, and histochemical studies. Bauhinia purpurea lectin (BPA) is a leguminous lectin with an affinity for galactose and lactose. Nine amino acids, DTWPNTEWS, corresponding to the amino acid sequence from aspartic acid-135 to serine-143 in the primary structure of BPA were replaced with the corresponding amino acid residues from the mannose-binding Lens culinaris lectin (LCA), and the chimeric lectin obtained was expressed in Escherichia coli cells. The carbohydrate-binding specificity of the recombinant chimeric lectin was investigated in detail by comparing the elution profiles of various glycopeptides and oligosaccharides with defined carbohydate structures from immobilized lectin columns. Glycopeptides carrying three constitutive carbohydrate sequences of Galbeta1-3GalNAc-Ser/Thr and a complex-type biantennary glycopeptide, which show a high affinity for BPA or LCA, were shown to have no affinity for the chimeric lectin. In contrast, hybrid-type and high mannose-type glycopeptides with a Manalpha1-6(Manalpha1-3)Manalpha1-6Man sequence were found to have a moderate affinity for the chimeric lectin. This result demonstrates that a novel type of lectin with a unique carbohydrate-binding specificity can be constructed from BPA by substituting several amino acid residues in its metal-binding region with other amino acid residues. Additional lectin(s) with distinctly different carbohydrate-binding specificities will provide a powerful tool for many studies.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Abstract To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a d -galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose—Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the α- d -mannose binding Lens culinaris lectins. Although BPA is specific for β- d -galactose, the chimeric lectin expressed in Escherichia coli was found to bind α- d -mannosyl—bovine serum albumin and this binding was inhibited by d -mannose.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the alpha-D-mannose binding Lens culinaris lectins. Although BPA is specific for beta-D-galactose, the chimeric lectin expressed in Escherichia coli was found to bind alpha-D-mannosyl-bovine serum albumin and this binding was inhibited by D-mannose.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.
Journal of biochemistry, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind alpha mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose.
Yukiko Konami - One of the best experts on this subject based on the ideXlab platform.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin
2016Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-bindlng Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind a mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose. Lectins are carbohydrate-binding proteins and are particu-larly abundant in the seeds of leguminous plants (1, 2). Although the various legume lectins have different carbo-hydrate specificities, a high homology was found among the amino acid sequences of these lectins (3-16). The Bauhinia purpurea lectin (BPA) is specific for galactose and lactose, and binds Galy31-3GalNAc preferentially (17). We have already determined the complete amino acid sequence of BPA by means of cDNA cloning (8). To elucidate the correlation between the amino aci
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A chimeric lectin formed from Bauhinia purpurea lectin and Lens culinaris lectin recognizes a unique carbohydrate structure.
Journal of biochemistry, 2000Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Lectins are carbohydrate-binding proteins widely used in biochemical, immunochemical, and histochemical studies. Bauhinia purpurea lectin (BPA) is a leguminous lectin with an affinity for galactose and lactose. Nine amino acids, DTWPNTEWS, corresponding to the amino acid sequence from aspartic acid-135 to serine-143 in the primary structure of BPA were replaced with the corresponding amino acid residues from the mannose-binding Lens culinaris lectin (LCA), and the chimeric lectin obtained was expressed in Escherichia coli cells. The carbohydrate-binding specificity of the recombinant chimeric lectin was investigated in detail by comparing the elution profiles of various glycopeptides and oligosaccharides with defined carbohydate structures from immobilized lectin columns. Glycopeptides carrying three constitutive carbohydrate sequences of Galbeta1-3GalNAc-Ser/Thr and a complex-type biantennary glycopeptide, which show a high affinity for BPA or LCA, were shown to have no affinity for the chimeric lectin. In contrast, hybrid-type and high mannose-type glycopeptides with a Manalpha1-6(Manalpha1-3)Manalpha1-6Man sequence were found to have a moderate affinity for the chimeric lectin. This result demonstrates that a novel type of lectin with a unique carbohydrate-binding specificity can be constructed from BPA by substituting several amino acid residues in its metal-binding region with other amino acid residues. Additional lectin(s) with distinctly different carbohydrate-binding specificities will provide a powerful tool for many studies.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:Abstract To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a d -galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose—Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the α- d -mannose binding Lens culinaris lectins. Although BPA is specific for β- d -galactose, the chimeric lectin expressed in Escherichia coli was found to bind α- d -mannosyl—bovine serum albumin and this binding was inhibited by d -mannose.
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determination of the carbohydrate binding site of Bauhinia purpurea lectin by affinity chromatography
Journal of Chromatography A, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki OsawaAbstract:To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and its amino acid sequence is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment with the ability to interact with lactose was also purified and found to contain this sequence, consisting of nine amino acids. This nonapeptide was aligned in a part of the metal-binding region conserved in all legume lectins. The chemical synthesis of the nonapeptide was carried out by a solid-phase method and the synthetic peptide showed a lactose-specific binding activity in the presence of calcium. A chimeric lectin gene was constructed using a cDNA coding BPA in which the nonapeptide sequence was replaced by the corresponding region of the alpha-D-mannose binding Lens culinaris lectins. Although BPA is specific for beta-D-galactose, the chimeric lectin expressed in Escherichia coli was found to bind alpha-D-mannosyl-bovine serum albumin and this binding was inhibited by D-mannose.
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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.
Journal of biochemistry, 1992Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro IrimuraAbstract:A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind alpha mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose.
Mohd Zaki Salleh - One of the best experts on this subject based on the ideXlab platform.
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hepatoprotective action of various partitions of methanol extract of Bauhinia purpurea leaves against paracetamol induced liver toxicity involvement of the antioxidant mechanisms
BMC Complementary and Alternative Medicine, 2016Co-Authors: Zainul Amiruddin Zakaria, Farhana Yahya, Nur Diyana Mahmood, Norhafizah Mohtarrudin, Lay Kek Teh, Siti Syariah Mamat, Muhammad Taher, Siti Selina Abdul Hamid, Mohd Zaki SallehAbstract:Background Methanol extract of Bauhinia purpurea L. (family Fabaceae) (MEBP) possesses high antioxidant and anti-inflammatory activities and recently reported to exert hepatoprotection against paracetamol (PCM)-induced liver injury in rats. In an attempt to identify the hepatoprotective bioactive compounds in MEBP, the extract was prepared in different partitions and subjected to the PCM-induced liver injury model in rats.
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in vivo antiulcer activity of the aqueous extract of Bauhinia purpurea leaf
Journal of Ethnopharmacology, 2011Co-Authors: Z A Zakaria, E Abdul E Hisam, M S Rofiee, M Norhafizah, M N Somchit, Lay Kek Teh, Mohd Zaki SallehAbstract:Abstract Ethnopharmacological relevance Bauhinia purpurea (Fabaceae) is a medicinal plant traditionally used to treat various ailments, including ulcers. In order to establish pharmacological properties of the leaf of Bauhinia purpurea, studies were performed on antiulcer activity of the plant's aqueous extract. Materials and methods The Bauhinia purpurea aqueous extract (BPAE) was prepared in the doses of 100, 500 and 1000 mg/kg. Antiulcer activity of BPAE was evaluated by absolute ethanol- and indomethacin-induced gastric ulcer, and pyloric ligation models. Acute toxicity was also carried out. Results BPAE, at the dose of 5000 mg/kg, did not cause any signs of toxicity to rats when given orally. Oral administration of BPAE exhibited antiulcer activity (p Conclusions The BPAE exhibits antiulcer activity, which could be due to the presence of saponins or sugar-free polyphenols, and, thus, confirmed the traditional uses of Bauhinia purpurea in the treatment of ulcers.
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Bauhinia purpurea leaves extracts exhibited in vitro antiproliferative and antioxidant activities
African Journal of Biotechnology, 2011Co-Authors: Zuki Abu Bakar Zakaria, M S Rofiee, Lay Kek Teh, Mohd Zaki Salleh, Mohd Roslan Sulaiman, M N SomchitAbstract:The antiproliferative and antioxidant activities of various extracts of the leaves of Bauhinia purpurea were studied using in vitro standard assays. The aqueous and chloroform extracts successfully inhibited the proliferation of all cancer cells while the methanol extract inhibited the proliferation of all cells except the CEMss cells when assessed using the 3,(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) (MTT) assay. The aqueous extract was effective against MCF-7 (IC 50 ≈ 9 μg/ml), MDA-MB 231 (IC 50 ≈ 17 μg/ml) and Caov-3 (IC 50 ≈ 16 μg/ml); the chloroform extract was highly effective against the CEMss (IC 50 ≈ 18 μg/ml) and HeLa (IC 50 ≈ 21 μg/ml); and the methanol extract was highly effective only against the HL-60 (≈ 12 μg/ml) cell lines. Interestingly, all extracts did not inhibit the proliferation of 3T3 cells suggesting their non-cytotoxic properties. The aqueous and methanol, but not chloroform, extracts of B. purpurea (20, 100 and 500 μg/ml) exhibited concentration-dependent antioxidant activity only in the superoxide scavenging assay, but low to moderate activity in the 2,2- diphenyl-1 picrylhydrazyl (DPPH) radical scavenging assay, which could be associated with their total phenolic contents. In conclusion, the B. purpurea leaf possesses potential antiproliferative and concentration-dependent antioxidant activities. Purification and determination of active compounds are required for further study. Keywords: Bauhinia purpurea , in vitro , antiproliferative activity, antioxidant activity, phenolic compounds
Kristijanto A. Ign. - One of the best experts on this subject based on the ideXlab platform.
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Karakterisasi dan Komposisi Kimia Minyak Biji Tumbuhan Kupu-Kupu (Bauhinia purpurea L.) Bunga Merah Muda
Fakultas Sains dan Matematika Universitas Kristen Satya Wacana, 2014Co-Authors: Dewi, Mega E. Kurnia, Soetjipto Hartati, Kristijanto A. Ign.Abstract:Prosiding Seminar Nasional Sains dan Pendidikan Sains IX, Fakultas Sains dan Matematika UKSW Salatiga, 21 Juni 2014, Vol 5, No.1, p. K11 - 17Studi karakterisasi dan komposisi minyak biji tumbuhan kupu-kupu (Bauhinia purpurea L.) telah dilakukan di Laboratorium Kimia FSM UKSW, Salatiga. Tujuan dari penelitian ini adalah untuk menentukan sifat fisiko-kimiawi dan komposisi minyak biji B. purpurea bunga merah muda. Ekstraksi dilakukan dengan metode soxhletasi selama enam jam dengan pelarut heksana lalu minyak yang diperoleh dikarakterisasi parameter fisiko-kimiawi, sedangkan analisa komposisi minyak dilakukan dengan GCMS. Sifat fisikawi minyak biji tumbuhan kupu-kupu bunga merah muda antara lain: berwarna kuning, berbau khas dan memiliki massa jenis 0,5882 g/cm3. Sifat kimiawi minyak biji tumbuhan kupu kupu bunga merah muda antara lain: pH 6, bilangan asam 12,59 mg KOH/g sampel, bilangan peroksida 50,02 mgrek oksigen/ kg sampel dan bilangan saponifikasi 100,40 mg KOH/g sampel. Hasil analisisis GCMS, menunjukkan komposisi kimia minyak biji B. purpurea bunga merah muda didominasi oleh asam linoleat (51,32%) dan asam palmitat (29,31%
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Pengaruh Lama Ekstraksi Terhadap Rendemen dan Parameter Fisiko-Kimiawi Minyak Biji Tumbuhan Kupu-kupu (Bauhinia purpurea L.)
Fakultas Sains dan Matematika Universitas Kristen Satya Wacana, 2014Co-Authors: Dewi, Mega E. Kurnia, Soetjipto Hartati, Kristijanto A. Ign.Abstract:Prosiding Seminar Nasional Sains dan Pendidikan Sains IX, Fakultas Sains dan Matematika UKSW Salatiga, 21 Juni 2014, Vol 5, No.1, p. K6 - 10Studi pengaruh lama waktu ekstraksi terhadap rendemen dan parameter fisiko-kimiawi minyak biji tumbuhan kupu-kupu (Bauhinia purpurea L.) telah dilakukan di Laboratorium Kimia Bahan Alam FSM UKSW, Salatiga. Tujuan dari penelitian adalah untuk menentukan pengaruh lama waktu ekstraksi terhadap rendemen dan sifat fisiko-kimiawi minyak biji B. purpurea bunga merah muda. Ekstraksi dilakukan dengan metode soxhletasi selama 4,5 sampai 7,5 jam dengan pelarut heksana lalu minyak yang diperoleh dikarakterisasi parameter fisiko-kimiawi. Data dianalisis dengan menggunakan Rancangan Acak Kelompok (RAK), 3 perlakuan dan 9 ulangan. Sebagai perlakuan adalah lama waktu ekstraksi (4,5; 6,0 dan 7,5 jam) dan sebagai kelompok adalah waktu analisis. Pengujian antar rataan perlakuan dilakukan dengan menggunakan uji Beda Nyata Jujur (BNJ) dengan tingkat kebermaknaan 5 %. Hasil penelitian menunjukkan bahwa lama waktu ekstraksi 7,5 jam menurunkan bilangan peroksida minyak biji tumbuhan kupu-kupu. Sebaliknya, lama waktu ekstraksi tidak berpengaruh terhadap rendemen, kadar air, bilangan asam dan bilangan penyabunan minya
