Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.89
H. Yoshii, T. Furuta, Miyuki Ikeda, Y. Nakagawa, H. Hirano, Yuichi Maeda, Y. Linko, P. Linko
Okara is a by-product of tofu and soybean protein production. Okara contains 80-85% moisture. The dehydration of okara is very difficult with the conventional method. In the present work, okara was dehydrated with a compression instrument (0.49 MPa) using calcium chloride. About 65% water content, on a wet basis, could be obtained with the addition of calcium chloride at levels higher than 0.01 g/g of wet okara. The water content of the dehydrated okara correlated with the pH of the dehydrated solution obtained by dehydration with calcium chloride. With 2% calcium chloride solution, water contents less than 67% could be obtained during four repeated dehydration cycles.
{"title":"Dehydration of Okara with Calcium Chloride","authors":"H. Yoshii, T. Furuta, Miyuki Ikeda, Y. Nakagawa, H. Hirano, Yuichi Maeda, Y. Linko, P. Linko","doi":"10.3136/FSTI9596T9798.4.89","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.89","url":null,"abstract":"Okara is a by-product of tofu and soybean protein production. Okara contains 80-85% moisture. The dehydration of okara is very difficult with the conventional method. In the present work, okara was dehydrated with a compression instrument (0.49 MPa) using calcium chloride. About 65% water content, on a wet basis, could be obtained with the addition of calcium chloride at levels higher than 0.01 g/g of wet okara. The water content of the dehydrated okara correlated with the pH of the dehydrated solution obtained by dehydration with calcium chloride. With 2% calcium chloride solution, water contents less than 67% could be obtained during four repeated dehydration cycles.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"16 1","pages":"89-93"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75057014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.59
K. Kaneko, C. Otoguro, Norihiko Yoshida, Makoto Utada, K. Tsuji, S. Kikuchi, Hawan-Soo Cha
{"title":"Influence of the Maturity of the Fruit Material on Various Components and Taste of Ume Liquor","authors":"K. Kaneko, C. Otoguro, Norihiko Yoshida, Makoto Utada, K. Tsuji, S. Kikuchi, Hawan-Soo Cha","doi":"10.3136/FSTI9596T9798.4.59","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.59","url":null,"abstract":"","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"16 1","pages":"59-65"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72808211","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.18
Kimio Nishimura, N. Imazuya, S. Nakai
When cream puff paste (CPP) was baked after it was kept at 35°C for 3 h, it did not puff up as much as one baked just after preparation of the CPP. The optimum preparative method for CPP with the least deterioration during storage was found by carrying out random centroid optimization regarding 9 factors, such as the ratio of flour, shortening, yolk, egg white and water as ingredients, and the heating time at the first stage, the temperature of the heated mixture of water, shortening, and flour on the addition of the egg solution, and the time and temperature of the incubation of the yolk as preparative conditions. The optimum values of 18.0%, 14.7%, 13.4%, 25.4%, 28.5%, 106.5s, 53.9°C, 46.7 min, and 63.7°C were obtained, respectively. Each value except the time and temperature for incubating the yolk was similar to that in the standard preparative method of CPP, which brought about deterioration during storage. The incubation of the yolk at 63.7°C for 46.7 min caused a decreased in the specific activity of amylase in the yolk from 1.71±0.43 to 0.20±0.17 μg of maltose/mg of protein but did not affect proteins in the CPP.
{"title":"Optimum Preparative Method for Storing Cream Puff Paste without Deterioration.","authors":"Kimio Nishimura, N. Imazuya, S. Nakai","doi":"10.3136/FSTI9596T9798.4.18","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.18","url":null,"abstract":"When cream puff paste (CPP) was baked after it was kept at 35°C for 3 h, it did not puff up as much as one baked just after preparation of the CPP. The optimum preparative method for CPP with the least deterioration during storage was found by carrying out random centroid optimization regarding 9 factors, such as the ratio of flour, shortening, yolk, egg white and water as ingredients, and the heating time at the first stage, the temperature of the heated mixture of water, shortening, and flour on the addition of the egg solution, and the time and temperature of the incubation of the yolk as preparative conditions. The optimum values of 18.0%, 14.7%, 13.4%, 25.4%, 28.5%, 106.5s, 53.9°C, 46.7 min, and 63.7°C were obtained, respectively. Each value except the time and temperature for incubating the yolk was similar to that in the standard preparative method of CPP, which brought about deterioration during storage. The incubation of the yolk at 63.7°C for 46.7 min caused a decreased in the specific activity of amylase in the yolk from 1.71±0.43 to 0.20±0.17 μg of maltose/mg of protein but did not affect proteins in the CPP.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"22 1","pages":"18-24"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80930099","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.33
S. Furuta, I. Suda, Y. Nishiba, O. Yamakawa
The tert-butylperoxyl radical (t-BuOO·) scavenging activities of ethanol extracts of 21 sweet potato cultivars with several flesh colors were examined using a tert-butyl hydroperoxide (t-BuOOH)/hemin/luminol system. Among them, sweet potato cultivars with purple flesh, which contained anthocyanins, had the highest t-BuOO· scavenging activities. Those cultivars with purple flesh also had the highest antioxidative activities against lipid peroxidation induced by auto-oxidation of linoleic acid. Most of the sweet potato cultivars with white, white-yellow, yellow and orange flesh had low t-BuOO· scavenging and antioxidative activities; however, some of them had higher activities. In all sweet potato cultivars tested, the t-BuOO· scavenging activities became higher with an increase in the total phenolic content.
{"title":"High tert-Butylperoxyl Radical Scavenging Activities of Sweet Potato Cultivars with Purple Flesh","authors":"S. Furuta, I. Suda, Y. Nishiba, O. Yamakawa","doi":"10.3136/FSTI9596T9798.4.33","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.33","url":null,"abstract":"The tert-butylperoxyl radical (t-BuOO·) scavenging activities of ethanol extracts of 21 sweet potato cultivars with several flesh colors were examined using a tert-butyl hydroperoxide (t-BuOOH)/hemin/luminol system. Among them, sweet potato cultivars with purple flesh, which contained anthocyanins, had the highest t-BuOO· scavenging activities. Those cultivars with purple flesh also had the highest antioxidative activities against lipid peroxidation induced by auto-oxidation of linoleic acid. Most of the sweet potato cultivars with white, white-yellow, yellow and orange flesh had low t-BuOO· scavenging and antioxidative activities; however, some of them had higher activities. In all sweet potato cultivars tested, the t-BuOO· scavenging activities became higher with an increase in the total phenolic content.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"114 1","pages":"33-35"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87964359","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.44
Y. Miyaguchi, M. Tsutsumi, Kiyomi Nagayama
Peptic globin digest (PG) was prepared from porcine blood globin, and the peptides were characterized by separation processes such as gel filtration chromatography, hydrophobic chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Aggregation of the peptides was indicated by highperformance liquid chrornatography (HPLC). Two fractions (FI and F2) were obtained from PG by gel filtration chromatography. Hydrophobic chromatography of fraction F1 was carried out, and a peak corresponding to the aggregate was found in fractions Flb-Fle. These fractions, which showed an aggregate peak by HPLC, were subjected to SDS-PAGE, and two major peptide bands with molecular weight of 5000 and 6000 were found. Amino acid sequence indicated the N-terminal amino acid of these peptides to be 42-47 (Phe-Asp) and 86-92 (Ala-Leu) of p-globin, respectively. Furthermore, it was predicted that the Mw 5000 and 6000 peptides may possibly be 42-85 (MW 4749) and 86-141 (MW 6117) of p-globin, respectively, based on the specificity of pepsin.
{"title":"Aggregate Formation of Peptic Globin Digest.","authors":"Y. Miyaguchi, M. Tsutsumi, Kiyomi Nagayama","doi":"10.3136/FSTI9596T9798.4.44","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.44","url":null,"abstract":"Peptic globin digest (PG) was prepared from porcine blood globin, and the peptides were characterized by separation processes such as gel filtration chromatography, hydrophobic chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Aggregation of the peptides was indicated by highperformance liquid chrornatography (HPLC). Two fractions (FI and F2) were obtained from PG by gel filtration chromatography. Hydrophobic chromatography of fraction F1 was carried out, and a peak corresponding to the aggregate was found in fractions Flb-Fle. These fractions, which showed an aggregate peak by HPLC, were subjected to SDS-PAGE, and two major peptide bands with molecular weight of 5000 and 6000 were found. Amino acid sequence indicated the N-terminal amino acid of these peptides to be 42-47 (Phe-Asp) and 86-92 (Ala-Leu) of p-globin, respectively. Furthermore, it was predicted that the Mw 5000 and 6000 peptides may possibly be 42-85 (MW 4749) and 86-141 (MW 6117) of p-globin, respectively, based on the specificity of pepsin.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"234 1","pages":"44-47"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76109298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.36
Shaohui Zhang, K. Imada, T. Ohashi
A pilot plant, with immobilized β-galactosidase (IMG) in a plug flow reactor, was established to prepare whey syrup from cheese whey. The effects of space velocity and lactose concentration on the initial rate of lactose hydrolysis (IRLH) and the operational temperature effect on the half-life and productivity of IMG were investigated. When the space velocity of whey was controlled at 0.6 l/(l·min), consolidation and channeling did not occur in the pilot plant. A better IRLH was obtained when the whey had high lactose concentration. With an increase in operational temperature in the pilot plant, the IRLH was increased. However, the half-life of IMG was shortened, as a result, the productivity of IMG decreased. The best temperature was 10°C for the operation of the pilot plant. The plant could be operated for as long as 50 days at 10°C if the IMG is washed by sterilized deionized water for 1 h each day. When the IRLH decreases to 10%, the IMG is treated by phosphate buffer solution (0.01 M, pH 6.4) and tetramethylammonium chloride solution (0.03%, pH 2.5) for 30 min, respectively. These results show that the developed pilot plant had prospects in the dairy industry because it could be operated continuously for a long period, the washing and sterilization were simple, and the rate of lactose hydrolysis (RLH) was more than 80% in the whey syrup.
采用塞流反应器固定化β-半乳糖苷酶(IMG)制备干酪乳清糖浆。考察了空速和乳糖浓度对乳糖水解初始速率(IRLH)的影响以及操作温度对IMG半衰期和产率的影响。当乳清空速控制在0.6 l/(l·min)时，中试装置不发生固结和窜槽现象。当乳清的乳糖浓度较高时，IRLH较好。随着中试装置运行温度的升高，IRLH也随之升高。但IMG的半衰期缩短，导致生产效率下降。中试装置的最佳运行温度为10℃。如果每天用消过毒的去离子水洗涤IMG 1小时，则可在10°C下运行长达50天。当IRLH降至10%时，分别用磷酸盐缓冲液(0.01 M, pH 6.4)和四甲基氯化铵溶液(0.03%，pH 2.5)处理IMG 30min。结果表明，该装置可长时间连续运行，清洗杀菌简单，乳清糖浆中乳糖水解率可达80%以上，在乳制品工业中具有广阔的应用前景。
{"title":"Preparation of Whey Syrup by Immobilized β-Galactosidase","authors":"Shaohui Zhang, K. Imada, T. Ohashi","doi":"10.3136/FSTI9596T9798.4.36","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.36","url":null,"abstract":"A pilot plant, with immobilized β-galactosidase (IMG) in a plug flow reactor, was established to prepare whey syrup from cheese whey. The effects of space velocity and lactose concentration on the initial rate of lactose hydrolysis (IRLH) and the operational temperature effect on the half-life and productivity of IMG were investigated. When the space velocity of whey was controlled at 0.6 l/(l·min), consolidation and channeling did not occur in the pilot plant. A better IRLH was obtained when the whey had high lactose concentration. With an increase in operational temperature in the pilot plant, the IRLH was increased. However, the half-life of IMG was shortened, as a result, the productivity of IMG decreased. The best temperature was 10°C for the operation of the pilot plant. The plant could be operated for as long as 50 days at 10°C if the IMG is washed by sterilized deionized water for 1 h each day. When the IRLH decreases to 10%, the IMG is treated by phosphate buffer solution (0.01 M, pH 6.4) and tetramethylammonium chloride solution (0.03%, pH 2.5) for 30 min, respectively. These results show that the developed pilot plant had prospects in the dairy industry because it could be operated continuously for a long period, the washing and sterilization were simple, and the rate of lactose hydrolysis (RLH) was more than 80% in the whey syrup.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"20 1","pages":"36-39"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75347277","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.9
M. Ono, C. Masuoka, Yasuyuki Ito, T. Nohara
Seven phenolic compounds, vanillic acid (1), threo-guaiacyl glycerol (2), erythro-guaiacyl glycerol (3), taxifolin (4), dihydrodehydrodiconiferyl alcohol (5), dihydrodehydrodiconiferyl alcohol-9-O-β-D-glucoside (6) and dihydrodehydrodiconiferyl alcohol-(4→8)-erythro-guaiacyl glycerol ether (7), were separated from the methanol extract of Viticis trifoliae Fructus (Fruit of Vitex rotundifolia L.) and their structures were identified on the basis of spectroscopic data. In addition, 1, 2, 4-7 and two previously isolated iridoid glucosides, agnuside (8) and VR-I (10-O-vanilloyl aucubin) (9) were tested for antioxidative activity using the ferric thiocyanate method. These compounds, except 8, exhibited stronger antioxidative activity than 3-tert-butyl-4-hydroxyanisole. Moreover, 1, 2 and 4-9 were investigated for the scavenging effect on 1,1-diphenyl-2-picrylhydrazyl. All tested compounds, except 8, showed a potent scavenging effect. Especially, the effect of 4 was almost twice that of α-tocopherol at a concentration of 0.02 mM.
从三叶葡萄(Viticis trifoliae Fructus)甲醇提取物中分离得到香草酸(1)、三愈创木酰甘油(2)、红愈创木酰甘油(3)、杉木素(4)、二氢脱氢二银叶醇(5)、二氢脱氢二银叶醇-9- o- β- d -葡萄糖苷(6)和二氢脱氢二银叶醇-(4→8)-红愈创木酰甘油醚(7)7个酚类化合物，并通过波谱分析对其结构进行了鉴定。此外，1,2,4 -7和先前分离的两种环烯醚萜苷，agnuside(8)和VR-I (10- o -香草叶红桃素)(9)使用铁硫氰酸盐方法测试了抗氧化活性。除8外，其余化合物的抗氧化活性均高于3-叔丁基-4-羟基茴香醚。此外，还研究了1、2和4-9对1,1-二苯基-2-苦味酰肼的清除作用。除8种化合物外，其余化合物均有清除作用。特别是在浓度为0.02 mM时，4的效果几乎是α-生育酚的两倍。
{"title":"Antioxidative Constituents from Viticis trifoliae Fructus (Fruit of Vitex rotundifolia L.)","authors":"M. Ono, C. Masuoka, Yasuyuki Ito, T. Nohara","doi":"10.3136/FSTI9596T9798.4.9","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.9","url":null,"abstract":"Seven phenolic compounds, vanillic acid (1), threo-guaiacyl glycerol (2), erythro-guaiacyl glycerol (3), taxifolin (4), dihydrodehydrodiconiferyl alcohol (5), dihydrodehydrodiconiferyl alcohol-9-O-β-D-glucoside (6) and dihydrodehydrodiconiferyl alcohol-(4→8)-erythro-guaiacyl glycerol ether (7), were separated from the methanol extract of Viticis trifoliae Fructus (Fruit of Vitex rotundifolia L.) and their structures were identified on the basis of spectroscopic data. In addition, 1, 2, 4-7 and two previously isolated iridoid glucosides, agnuside (8) and VR-I (10-O-vanilloyl aucubin) (9) were tested for antioxidative activity using the ferric thiocyanate method. These compounds, except 8, exhibited stronger antioxidative activity than 3-tert-butyl-4-hydroxyanisole. Moreover, 1, 2 and 4-9 were investigated for the scavenging effect on 1,1-diphenyl-2-picrylhydrazyl. All tested compounds, except 8, showed a potent scavenging effect. Especially, the effect of 4 was almost twice that of α-tocopherol at a concentration of 0.02 mM.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"16 1","pages":"9-13"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88149880","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1998-02-25DOI: 10.3136/FSTI9596T9798.4.40
Y. Miyaguchi, M. Tsutsumi, Kiyomi Nagayama
The effects of pepsin treatment on the gelation of porcine globin were studied by measurements of surface hydrophobicity, extent of hydrolysis, gel strength and polyacrylamide gel electrophoresis. Gel formation occurred below pH 4.0 at 30-50°C above 3% globin concentration. After 48-h incubation at pH 3.0 and 50°C in the pepsin concentration used (0.005-1.0% (E/S)), 0.01% (enzyme-substrate ratio: E/S) pepsin gave the highest gel strength. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed several peptides with molecular weight of 4000-6000 to be present in the resultant gel after 48 h of pepsin treatment. Gel strength after 12-h incubation was highly correlated with surface hydrophobicity and markedly elevated at 2-3% hydrolysis. As longer incubation time (over 12 h) is required for maximum gel strength, the gelation of globin would thus appear to occur as follows: pepsin yields peptides from globin, which aggregate to produce a three-dimensional gel network during incubation.
{"title":"Gelation of Porcine Globin by Pepsin Treatment","authors":"Y. Miyaguchi, M. Tsutsumi, Kiyomi Nagayama","doi":"10.3136/FSTI9596T9798.4.40","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.4.40","url":null,"abstract":"The effects of pepsin treatment on the gelation of porcine globin were studied by measurements of surface hydrophobicity, extent of hydrolysis, gel strength and polyacrylamide gel electrophoresis. Gel formation occurred below pH 4.0 at 30-50°C above 3% globin concentration. After 48-h incubation at pH 3.0 and 50°C in the pepsin concentration used (0.005-1.0% (E/S)), 0.01% (enzyme-substrate ratio: E/S) pepsin gave the highest gel strength. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed several peptides with molecular weight of 4000-6000 to be present in the resultant gel after 48 h of pepsin treatment. Gel strength after 12-h incubation was highly correlated with surface hydrophobicity and markedly elevated at 2-3% hydrolysis. As longer incubation time (over 12 h) is required for maximum gel strength, the gelation of globin would thus appear to occur as follows: pepsin yields peptides from globin, which aggregate to produce a three-dimensional gel network during incubation.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"217 1","pages":"40-43"},"PeriodicalIF":0.0,"publicationDate":"1998-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74965839","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1997-11-25DOI: 10.3136/FSTI9596T9798.3.393
Mir Nurul Momen, Y. Tatsumi, K. Shimokawa
The effects of a 2% sucrose palmitic acid ester coating were studied on the internal oxygen, carbon dioxide and ethylene concentrations of banana fruits in relation to ripening, respiration and ethylene production during storage at 20°C after treatment with 100 ppm ethylene for 12 h. The 2% sucrose palmitic acid ester coating on the bananas covered the stomatal aperture, suppressed initial respiration and decreased the rate of ethylene production which ultimately retarded degreening and significantly delayed (P<0.01) ripening. The internal oxygen concentration of the bananas was significantly (P<0.05) reduced by the coating treatment without elevation of the internal carbon dioxide level. Low internal oxygen concentration significantly reduced (P<0.01) the rate of ethylene production of the coated bananas during 9 days in storage. These observations indicated that coating with the sucrose palmitic acid ester modified the internal atmosphere of banana fruits and suppressed initial respiration in a manner analogous to modified atmosphere storage.
{"title":"Effects of Sucrose Palmitic Acid Ester Coating on the Internal Gas Concentrations of Cavendish Bananas in Relation to the Ripening, Respiration and Ethylene Production.","authors":"Mir Nurul Momen, Y. Tatsumi, K. Shimokawa","doi":"10.3136/FSTI9596T9798.3.393","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.3.393","url":null,"abstract":"The effects of a 2% sucrose palmitic acid ester coating were studied on the internal oxygen, carbon dioxide and ethylene concentrations of banana fruits in relation to ripening, respiration and ethylene production during storage at 20°C after treatment with 100 ppm ethylene for 12 h. The 2% sucrose palmitic acid ester coating on the bananas covered the stomatal aperture, suppressed initial respiration and decreased the rate of ethylene production which ultimately retarded degreening and significantly delayed (P<0.01) ripening. The internal oxygen concentration of the bananas was significantly (P<0.05) reduced by the coating treatment without elevation of the internal carbon dioxide level. Low internal oxygen concentration significantly reduced (P<0.01) the rate of ethylene production of the coated bananas during 9 days in storage. These observations indicated that coating with the sucrose palmitic acid ester modified the internal atmosphere of banana fruits and suppressed initial respiration in a manner analogous to modified atmosphere storage.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"80 1","pages":"393-397"},"PeriodicalIF":0.0,"publicationDate":"1997-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80961908","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1997-11-25DOI: 10.3136/FSTI9596T9798.3.388
T. Takeuchi, Y. Nibu, K. Murata, S. Yoshida, I. Kusakabe
An alginate lyase was purified from an extracellular enzyme (commercial preparation) of Flavobacterium multivolum K-11 by successive column chromatographies, such as cation exchange, chromatofocusing, and gel filtration. The purified enzyme migrated as a single band on SDS-PAGE and analytical isoelectric focusing. The molecular weight of the enzyme was 32,000 by SDS-PAGE and 33,000 by HPLC gel filtration chromatography, and the pI of the enzyme was 8.2 on isoelectric focusing. The enzyme exhibited maximum activity at pH 7.5 and 40°C, and was stable between pH 6.0 and 9.0, and at temperatures up to 20°C. The enzyme activity was remarkably inhibited by chemical compounds such as SDS, MIA, TNBS, and N-bromosuccinimide, while EDTA and PCMB had no effect on the enzyme activity. The enzyme decomposed both the G-block (guluronic acid content; 89%) and the M-block (mannuronic content; 92%) at nearly equal rates, and produced several kinds of unsaturated oligomers. Because such activity of alginate lyase has not been reported, we believe that this is a novel alginate lyase.
{"title":"Characterization of a Novel Alginate Lyase from Flavobacterium multivolum K-11","authors":"T. Takeuchi, Y. Nibu, K. Murata, S. Yoshida, I. Kusakabe","doi":"10.3136/FSTI9596T9798.3.388","DOIUrl":"https://doi.org/10.3136/FSTI9596T9798.3.388","url":null,"abstract":"An alginate lyase was purified from an extracellular enzyme (commercial preparation) of Flavobacterium multivolum K-11 by successive column chromatographies, such as cation exchange, chromatofocusing, and gel filtration. The purified enzyme migrated as a single band on SDS-PAGE and analytical isoelectric focusing. The molecular weight of the enzyme was 32,000 by SDS-PAGE and 33,000 by HPLC gel filtration chromatography, and the pI of the enzyme was 8.2 on isoelectric focusing. The enzyme exhibited maximum activity at pH 7.5 and 40°C, and was stable between pH 6.0 and 9.0, and at temperatures up to 20°C. The enzyme activity was remarkably inhibited by chemical compounds such as SDS, MIA, TNBS, and N-bromosuccinimide, while EDTA and PCMB had no effect on the enzyme activity. The enzyme decomposed both the G-block (guluronic acid content; 89%) and the M-block (mannuronic content; 92%) at nearly equal rates, and produced several kinds of unsaturated oligomers. Because such activity of alginate lyase has not been reported, we believe that this is a novel alginate lyase.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"71 1","pages":"388-392"},"PeriodicalIF":0.0,"publicationDate":"1997-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83964523","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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