Pub Date : 1999-08-01DOI: 10.1002/(SICI)1521-3803(19990801)43:4<245::AID-FOOD245>3.0.CO;2-#
W. Schütze, F. Mandel, H. Schulz
Es wird das Glucosinolat-Profil von Rettich (Raphanus sativus L.) sowie neuer Art- und Gattungsbastarde zwischen Raphanus sativus und Brassica oleracea mittels HPLC-UV und LC-MS untersucht. Die durch Vergleich mit Retentionszeiten und UV-Spektren von Standardsubstanzen getroffenen Zuordnungen der detektierten Komponenten konnten dabei mit Hilfe der LC-MS schnell und sicher bestatigt werden. Drei Glucosinolate (Glucoraphenin, Glucoerysolin und 4-Methylthiobutenylglucosinolat), die aufgrund ihrer teilweise hohen Konzentration in den Pflanzen sowohl fur die menschliche Ernahrung als auch fur die Resistenz der Brassica-Pflanzen von Bedeutung sein konnen, jedoch als Standardverbindungen kommerziell nicht zur Verfugung stehen, wurden mittels LC-MS charakterisiert. Die vorgestellten Untersuchungen zeigen, das sich die im API-ES Positiv-Modus durchgefuhrten LC-MS-Messungen sehr gut zur Identifizierung unbekannter Glucosinolate in pflanzlichem Material eignen. Die im Bereich der Zuchtungsforschung sowie der Qualitatskontrolle bestehenden Anwendungsmoglichkeiten werden diskutiert. Identification of glucosinolates in radish (Raphanus sativus L.) and cross-breeds of R. sativus L. x Brassica oleracea L. (Raphanobrassica) by LC-MS. The glucosinolate profiles in Raphanus sativus and new intergenetic as well as interspecific hybrids between Raphanus sativus and Brassica oleracea have been investigated by HPLC-UV and LC-MS. Tentative identification based on UV-spectra and retention times were confirmed by the indivdual LC-MS measurements. In this context three glucosinolates (glucoraphenin, glucoerysolin and 4-methylthiobutenyl glucosinolate), which are known for their nutritional and resistance value in the brassicaceae plants, but are not available as reference standards could be characterized by MS detection for the first time. The presented LC-MS analyses, performed in the API-ES positive mode, proved to be a very sensitive and selective method for the identification of unknown glucosinolates in plant material. Possible applications for breeding research as well as for quality control purposes are discussed.
{"title":"Identifizierung von Glucosinolaten in Rettich (Raphanus sativus L.) und Kreuzungen aus R. sativus L. x Brassica oleracea L. (Raphanobrassica) mittels LC-MS","authors":"W. Schütze, F. Mandel, H. Schulz","doi":"10.1002/(SICI)1521-3803(19990801)43:4<245::AID-FOOD245>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(19990801)43:4<245::AID-FOOD245>3.0.CO;2-#","url":null,"abstract":"Es wird das Glucosinolat-Profil von Rettich (Raphanus sativus L.) sowie neuer Art- und Gattungsbastarde zwischen Raphanus sativus und Brassica oleracea mittels HPLC-UV und LC-MS untersucht. Die durch Vergleich mit Retentionszeiten und UV-Spektren von Standardsubstanzen getroffenen Zuordnungen der detektierten Komponenten konnten dabei mit Hilfe der LC-MS schnell und sicher bestatigt werden. Drei Glucosinolate (Glucoraphenin, Glucoerysolin und 4-Methylthiobutenylglucosinolat), die aufgrund ihrer teilweise hohen Konzentration in den Pflanzen sowohl fur die menschliche Ernahrung als auch fur die Resistenz der Brassica-Pflanzen von Bedeutung sein konnen, jedoch als Standardverbindungen kommerziell nicht zur Verfugung stehen, wurden mittels LC-MS charakterisiert. Die vorgestellten Untersuchungen zeigen, das sich die im API-ES Positiv-Modus durchgefuhrten LC-MS-Messungen sehr gut zur Identifizierung unbekannter Glucosinolate in pflanzlichem Material eignen. Die im Bereich der Zuchtungsforschung sowie der Qualitatskontrolle bestehenden Anwendungsmoglichkeiten werden diskutiert. \u0000 \u0000 \u0000 \u0000Identification of glucosinolates in radish (Raphanus sativus L.) and cross-breeds of R. sativus L. x Brassica oleracea L. (Raphanobrassica) by LC-MS. The glucosinolate profiles in Raphanus sativus and new intergenetic as well as interspecific hybrids between Raphanus sativus and Brassica oleracea have been investigated by HPLC-UV and LC-MS. Tentative identification based on UV-spectra and retention times were confirmed by the indivdual LC-MS measurements. In this context three glucosinolates (glucoraphenin, glucoerysolin and 4-methylthiobutenyl glucosinolate), which are known for their nutritional and resistance value in the brassicaceae plants, but are not available as reference standards could be characterized by MS detection for the first time. The presented LC-MS analyses, performed in the API-ES positive mode, proved to be a very sensitive and selective method for the identification of unknown glucosinolates in plant material. Possible applications for breeding research as well as for quality control purposes are discussed.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"115 1","pages":"245-248"},"PeriodicalIF":0.0,"publicationDate":"1999-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80309729","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 : 1999-03-01DOI: 10.1002/(SICI)1521-3803(19990301)43:2<105::AID-FOOD105>3.0.CO;2-#
S. Rogacheva, Margarita J. Kuntcheva, I. Panchev, T. Obretenov
Nondialysable melanoidins have been isolated from the model systems L-ascorbic acid-L-glutamic acid. A comparison with L-ascorbic acid interactions with glycine and L-lysine has been made. The influence of reaction parameters on the formation of melanoidins has been studied. Their fractional and spectral characteristics and the kinetic thermodynamic parameters have been discussed.
不可透析的类黑素已从l -抗坏血酸- l -谷氨酸模型系统中分离出来。对l -抗坏血酸与甘氨酸和赖氨酸的相互作用进行了比较。研究了反应参数对类黑素生成的影响。讨论了它们的分数和光谱特性以及动力学热力学参数。
{"title":"Melanoidin formation in L-ascorbic acid-α-amino acids interaction. A comparative study","authors":"S. Rogacheva, Margarita J. Kuntcheva, I. Panchev, T. Obretenov","doi":"10.1002/(SICI)1521-3803(19990301)43:2<105::AID-FOOD105>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(19990301)43:2<105::AID-FOOD105>3.0.CO;2-#","url":null,"abstract":"Nondialysable melanoidins have been isolated from the model systems L-ascorbic acid-L-glutamic acid. A comparison with L-ascorbic acid interactions with glycine and L-lysine has been made. The influence of reaction parameters on the formation of melanoidins has been studied. Their fractional and spectral characteristics and the kinetic thermodynamic parameters have been discussed.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"16 1","pages":"105-108"},"PeriodicalIF":0.0,"publicationDate":"1999-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78649281","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 : 1998-10-01DOI: 10.1002/(SICI)1521-3803(199810)42:05<295::AID-FOOD295>3.3.CO;2-5
M. Khalil
Extraction and precipitation were investigated to determine the optimal conditions for preparation of protein concentrates from defatted melon seed kernels flour. Protein concentrates were prepared by extraction with distilled water, salt or alkaline solution. Alkaline solution led to the highest extraction yield of 84.5%. The protein concentrate has a good digestibility of 90.8% as determined by in vitro enzymatic method. The protein is rich in lysine 6.35% but poor in sulphur-containing amino acids such as methionine 0.27%, and cystine 0.33%. The protein isolate showed good whipping and emulsifying characteristics as well as water and oil absorptions.
{"title":"Factors affecting production of melon seed kernel protein: Yield, composition and protein isolates quality","authors":"M. Khalil","doi":"10.1002/(SICI)1521-3803(199810)42:05<295::AID-FOOD295>3.3.CO;2-5","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199810)42:05<295::AID-FOOD295>3.3.CO;2-5","url":null,"abstract":"Extraction and precipitation were investigated to determine the optimal conditions for preparation of protein concentrates from defatted melon seed kernels flour. Protein concentrates were prepared by extraction with distilled water, salt or alkaline solution. Alkaline solution led to the highest extraction yield of 84.5%. The protein concentrate has a good digestibility of 90.8% as determined by in vitro enzymatic method. The protein is rich in lysine 6.35% but poor in sulphur-containing amino acids such as methionine 0.27%, and cystine 0.33%. The protein isolate showed good whipping and emulsifying characteristics as well as water and oil absorptions.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"86 1","pages":"295-297"},"PeriodicalIF":0.0,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73229591","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 : 1998-10-01DOI: 10.1002/(SICI)1521-3803(199810)42:05<324::AID-FOOD324>3.3.CO;2-X
E. Finotti, F. Paoletti, A. Bertone, P. Galassi, G. Quaglia
{"title":"Antioxidant capacity determination of extra virgin olive oils unsaponifiable fraction by crocin bleaching inhibition method","authors":"E. Finotti, F. Paoletti, A. Bertone, P. Galassi, G. Quaglia","doi":"10.1002/(SICI)1521-3803(199810)42:05<324::AID-FOOD324>3.3.CO;2-X","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199810)42:05<324::AID-FOOD324>3.3.CO;2-X","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"42 1","pages":"324-325"},"PeriodicalIF":0.0,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75946000","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 : 1998-10-01DOI: 10.1002/(SICI)1521-3803(199810)42:05<302::AID-FOOD302>3.3.CO;2-C
Z. G. Narkiewicz-Jodko, M. Narkiewicz-Jodko
The aim of the research was the assessment of the milling and baking value of wheat cultivated after various fore-crops. Spring barley, rape, maize and pea were applied as fore-crops. It has been established that wheat cultivated after spring barley was characterised by the worst technological value. The largest amount of flour was obtained from wheat grain cultivated after maize and rape. Maize and rape used as fore-crops proved to have a favourable effect upon baking value of the flour.
{"title":"The effect of the fore-crop upon winter wheat milling and baking values","authors":"Z. G. Narkiewicz-Jodko, M. Narkiewicz-Jodko","doi":"10.1002/(SICI)1521-3803(199810)42:05<302::AID-FOOD302>3.3.CO;2-C","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199810)42:05<302::AID-FOOD302>3.3.CO;2-C","url":null,"abstract":"The aim of the research was the assessment of the milling and baking value of wheat cultivated after various fore-crops. Spring barley, rape, maize and pea were applied as fore-crops. It has been established that wheat cultivated after spring barley was characterised by the worst technological value. The largest amount of flour was obtained from wheat grain cultivated after maize and rape. Maize and rape used as fore-crops proved to have a favourable effect upon baking value of the flour.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"48 1","pages":"302-303"},"PeriodicalIF":0.0,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74139647","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 : 1998-10-01DOI: 10.1002/(SICI)1521-3803(199810)42:05<286::AID-FOOD286>3.3.CO;2-5
E. E. Babiker, A. Kato
Sorghum protein was conjugated with dextran or galactomannan under controlled conditions (60 °C, 79% relative humidity), or cross-linked with transglutaminase (TGase) to improve the functional prop-erties. SDS-PAGE patterns showed that the conjugated and cross-linked proteins had higher molecular mass bands above the stacking gel. Although sorghum protein and its polysaccharide mixture were insoluble at pH 4 — 6, the polysaccharide conjugates were soluble at all level of pHs, despite being composed of higher molecular sizes. Heat stability of the polysaccharide conjugates was greatly improved in that there were no turbidity at 100 °C, while TGase-treated samples sup-pressed heat-induced aggregation up to 60 °C. The emulsifying proper-ties of the polysaccharide conjugates and TGase treated sample were also greatly improved.
{"title":"Improvement of the functional properties of sorghum protein by protein-polysaccharide and protein-protein complexes","authors":"E. E. Babiker, A. Kato","doi":"10.1002/(SICI)1521-3803(199810)42:05<286::AID-FOOD286>3.3.CO;2-5","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199810)42:05<286::AID-FOOD286>3.3.CO;2-5","url":null,"abstract":"Sorghum protein was conjugated with dextran or galactomannan under controlled conditions (60 °C, 79% relative humidity), or cross-linked with transglutaminase (TGase) to improve the functional prop-erties. SDS-PAGE patterns showed that the conjugated and cross-linked proteins had higher molecular mass bands above the stacking gel. Although sorghum protein and its polysaccharide mixture were insoluble at pH 4 — 6, the polysaccharide conjugates were soluble at all level of pHs, despite being composed of higher molecular sizes. Heat stability of the polysaccharide conjugates was greatly improved in that there were no turbidity at 100 °C, while TGase-treated samples sup-pressed heat-induced aggregation up to 60 °C. The emulsifying proper-ties of the polysaccharide conjugates and TGase treated sample were also greatly improved.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"34 1","pages":"286-289"},"PeriodicalIF":0.0,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74478575","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 : 1998-10-01DOI: 10.1002/(SICI)1521-3803(199810)42:05<309::AID-FOOD309>3.3.CO;2-L
H. Coşkun
The aim of this study was to determine and compare the microbiological, biochemical and sensory characteristics of herby cheese made with two different methods. In the first method (M1), milk and herbs were pasteurized at 65°C for 30 min, and Lactococcus lactis subsp. lactis and L. lactis subsp. cremoris were added as starter culture at an inoculum ratio of 1.5%. In the second method (M2), the conventional cheesemaking was applied. Microbiological and biochemical changes were monitored throughout the ripening period of 90 days. Samples were taken from cheeses on days 1, 15, 30, 60, and 90. At the end of ripening, sensory characteristics of cheeses manufactured with both methods were evaluated. The obtained results suggested that most changes in pH, titratable acidity, and dry matter contents of cheese varieties were not found to differ statistically significant, but the difference in salt content was significant (P < 0.01). Total aerobic count, lactic acid bacteria, Staphylococcus aureus, coliforms, moulds, yeasts, proteolytic and lipolytic microorganism counts were lower in M1 cheese samples than those of M2 cheese samples (P < 0.01). The numbers of psychrotrophic microorganism in both cheese types were not found to differ significantly. Moreover, the results suggested that there were significant differences (P < 0.01) in the degrees of proteolysis and lipolysis of the cheese varieties. High proteolysis and lipolysis rates were monitored in the traditional cheese samples. However, there were no significant differences between the sensory characteristics of cheese samples.
{"title":"Microbiological and biochemical changes in herby cheese during ripening","authors":"H. Coşkun","doi":"10.1002/(SICI)1521-3803(199810)42:05<309::AID-FOOD309>3.3.CO;2-L","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199810)42:05<309::AID-FOOD309>3.3.CO;2-L","url":null,"abstract":"The aim of this study was to determine and compare the microbiological, biochemical and sensory characteristics of herby cheese made with two different methods. In the first method (M1), milk and herbs were pasteurized at 65°C for 30 min, and Lactococcus lactis subsp. lactis and L. lactis subsp. cremoris were added as starter culture at an inoculum ratio of 1.5%. In the second method (M2), the conventional cheesemaking was applied. Microbiological and biochemical changes were monitored throughout the ripening period of 90 days. Samples were taken from cheeses on days 1, 15, 30, 60, and 90. At the end of ripening, sensory characteristics of cheeses manufactured with both methods were evaluated. The obtained results suggested that most changes in pH, titratable acidity, and dry matter contents of cheese varieties were not found to differ statistically significant, but the difference in salt content was significant (P < 0.01). Total aerobic count, lactic acid bacteria, Staphylococcus aureus, coliforms, moulds, yeasts, proteolytic and lipolytic microorganism counts were lower in M1 cheese samples than those of M2 cheese samples (P < 0.01). The numbers of psychrotrophic microorganism in both cheese types were not found to differ significantly. Moreover, the results suggested that there were significant differences (P < 0.01) in the degrees of proteolysis and lipolysis of the cheese varieties. High proteolysis and lipolysis rates were monitored in the traditional cheese samples. However, there were no significant differences between the sensory characteristics of cheese samples.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"27 1","pages":"309-313"},"PeriodicalIF":0.0,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88796552","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 : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<245::AID-FOOD245>3.3.CO;2-Q
S. Tömösközi, R. Lásztity, E. Süle, J. Gaugecz, J. Varga
Osborne-type protein fractions and alkaline wheat germ protein isolate were produced and the latter was modified by urea-treatment, reduction and re-oxidation. The effects of modification on the protein subunit structure and on functional properties were investigated. Emulsifying activity, emulsion stability, solubility and aromatic surface hydrophobicity of 'native' and modified products were determined. Usually, the functional properties of the wheat germ protein isolate and the fractions were lower compared to casein. The comparison of Osborne-fractions, showed that albumins and glutelins have better functional properties than those of alkaline isolation and the globulin fraction. The results of the modification processes used in this work show, that only the elimination of hydrogen bonds have significant effects on solubility, emulsifying stability and surface hydrophobicity. These results indicate that hydrogen bonds play a main role in the formation of wheat germ protein structure.
{"title":"Functional properties of 'native' and modified wheat germ protein isolates and fractions","authors":"S. Tömösközi, R. Lásztity, E. Süle, J. Gaugecz, J. Varga","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<245::AID-FOOD245>3.3.CO;2-Q","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<245::AID-FOOD245>3.3.CO;2-Q","url":null,"abstract":"Osborne-type protein fractions and alkaline wheat germ protein isolate were produced and the latter was modified by urea-treatment, reduction and re-oxidation. The effects of modification on the protein subunit structure and on functional properties were investigated. Emulsifying activity, emulsion stability, solubility and aromatic surface hydrophobicity of 'native' and modified products were determined. Usually, the functional properties of the wheat germ protein isolate and the fractions were lower compared to casein. The comparison of Osborne-fractions, showed that albumins and glutelins have better functional properties than those of alkaline isolation and the globulin fraction. The results of the modification processes used in this work show, that only the elimination of hydrogen bonds have significant effects on solubility, emulsifying stability and surface hydrophobicity. These results indicate that hydrogen bonds play a main role in the formation of wheat germ protein structure.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"27 1","pages":"245-247"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85079278","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 : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<155::AID-FOOD155>3.3.CO;2-Q
C. Larré, G. Deshayes, J. Lefebvre, Y. Popineau
A microbial transglutaminase (TGase), was used to add covalent bonds in glutens obtained from three near-isogenic lines differing in their high Mr glutenin subunits content. After TGase treatment, 29-45% of the total proteins remained soluble instead of 70-90% for the untreated glutens, due to the formation of large insoluble polymers as shown by SDS-PAGE. The enzymatic treatment was effective in making gels with high elastic modulus from all tested glutens: G' was increased from 10 to 50 times and G from 2 to 4 times. The dynamic moduli of the reaction products were less frequency dependent than those of the non treated gluten. Despite the low lysine content of the gluten, the formation of permanent connections reinforced the network structure and modified the viscoelasticity properties of gluten.
{"title":"Hydrated gluten modified by a transglutaminase","authors":"C. Larré, G. Deshayes, J. Lefebvre, Y. Popineau","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<155::AID-FOOD155>3.3.CO;2-Q","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<155::AID-FOOD155>3.3.CO;2-Q","url":null,"abstract":"A microbial transglutaminase (TGase), was used to add covalent bonds in glutens obtained from three near-isogenic lines differing in their high Mr glutenin subunits content. After TGase treatment, 29-45% of the total proteins remained soluble instead of 70-90% for the untreated glutens, due to the formation of large insoluble polymers as shown by SDS-PAGE. The enzymatic treatment was effective in making gels with high elastic modulus from all tested glutens: G' was increased from 10 to 50 times and G from 2 to 4 times. The dynamic moduli of the reaction products were less frequency dependent than those of the non treated gluten. Despite the low lysine content of the gluten, the formation of permanent connections reinforced the network structure and modified the viscoelasticity properties of gluten.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"4 1","pages":"155-157"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84018454","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 : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<171::AID-FOOD171>3.3.CO;2-Y
J. V. Komissarova
{"title":"Isolation of Kunitz trypsin inhibitors from soy whey","authors":"J. V. Komissarova","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<171::AID-FOOD171>3.3.CO;2-Y","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<171::AID-FOOD171>3.3.CO;2-Y","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"9 1","pages":"171-172"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74630860","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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