Pub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<248::AID-FOOD248>3.3.CO;2-E
U. Einhorn-Stoll
{"title":"Interactions of whey proteins with different pectins in O/W emulsions","authors":"U. Einhorn-Stoll","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<248::AID-FOOD248>3.3.CO;2-E","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<248::AID-FOOD248>3.3.CO;2-E","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"98 1","pages":"248-249"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76338792","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<215::AID-FOOD215>3.3.CO;2-1
L. Sijtsma, D. Tezera, J. Hustinx, J. Vereijken
A commercial pea protein isolate has been hydrolysed by enzymatic treatment and functional properties of the freeze-dried hydrolysates were evaluated. Hydrolysis significantly improved the pea protein solubility, which made it more or less comparable to that measured for a soy protein hydrolysate, and reduced its pH dependency. In addition, hydrolysis improved emulsifying activity approximately two-fold with the maximum occurring at degree of hydrolysis (DH) 3.7. Foam expansion was improved nearly three-fold at the slightly lower DH value of 2.5.
{"title":"Improvement of pea protein quality by enzymatic modification","authors":"L. Sijtsma, D. Tezera, J. Hustinx, J. Vereijken","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<215::AID-FOOD215>3.3.CO;2-1","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<215::AID-FOOD215>3.3.CO;2-1","url":null,"abstract":"A commercial pea protein isolate has been hydrolysed by enzymatic treatment and functional properties of the freeze-dried hydrolysates were evaluated. Hydrolysis significantly improved the pea protein solubility, which made it more or less comparable to that measured for a soy protein hydrolysate, and reduced its pH dependency. In addition, hydrolysis improved emulsifying activity approximately two-fold with the maximum occurring at degree of hydrolysis (DH) 3.7. Foam expansion was improved nearly three-fold at the slightly lower DH value of 2.5.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"22 1","pages":"215-216"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77839713","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<242::AID-FOOD242>3.3.CO;2-1
E. Süle, S. Tömösközi, G. Hajós
{"title":"Functional properties of enzymatically modified plant proteins","authors":"E. Süle, S. Tömösközi, G. Hajós","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<242::AID-FOOD242>3.3.CO;2-1","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<242::AID-FOOD242>3.3.CO;2-1","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"16 1","pages":"242-244"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87304893","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<173::AID-FOOD173>3.3.CO;2-Q
M. Vorob'ev
{"title":"General kinetic model of proteolysis","authors":"M. Vorob'ev","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<173::AID-FOOD173>3.3.CO;2-Q","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<173::AID-FOOD173>3.3.CO;2-Q","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"67 1","pages":"173-174"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83508942","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<201::AID-FOOD201>3.3.CO;2-L
A. Krzyżaniak, T. Burova, T. Haertlé, J. Barciszewski
Purification to homogeneity of 2S albumin storage protein from rape seeds (napin) was achieved and its secondary structure and conformational stability were characterised by circular dichroism (CD), and high-sensitivity differential scanning calorimetry (HS-DSC). Deconvolution of the far-UV CD spectrum of napin revealed about 25% of α-helix and 38% of β-sheet structure at neutral and slightly acid pH. HS-DSC data show a single peak of protein denaturation with maximum at 101°C and 88°C at pH 6.0 and 3.0, respectively. This discloses very high stability of napin tertiary structure. The thermal denaturation of napin is irreversible duc to secondary processes such as hydrophobic aggregation of the unfolded protein. The deconvolution of the transition profile at pH 3.0 carried out with assumption that napin aggregation does not contribute to the transition parameters allows to distinguish two constituent transitions which may be attributed to two different domains in napin folding.
{"title":"The structure and properties of Napin-seed storage protein from rape (Brassica napus L.)","authors":"A. Krzyżaniak, T. Burova, T. Haertlé, J. Barciszewski","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<201::AID-FOOD201>3.3.CO;2-L","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<201::AID-FOOD201>3.3.CO;2-L","url":null,"abstract":"Purification to homogeneity of 2S albumin storage protein from rape seeds (napin) was achieved and its secondary structure and conformational stability were characterised by circular dichroism (CD), and high-sensitivity differential scanning calorimetry (HS-DSC). Deconvolution of the far-UV CD spectrum of napin revealed about 25% of α-helix and 38% of β-sheet structure at neutral and slightly acid pH. HS-DSC data show a single peak of protein denaturation with maximum at 101°C and 88°C at pH 6.0 and 3.0, respectively. This discloses very high stability of napin tertiary structure. The thermal denaturation of napin is irreversible duc to secondary processes such as hydrophobic aggregation of the unfolded protein. The deconvolution of the transition profile at pH 3.0 carried out with assumption that napin aggregation does not contribute to the transition parameters allows to distinguish two constituent transitions which may be attributed to two different domains in napin folding.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"14 1","pages":"201-204"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73282742","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<254::AID-FOOD254>3.3.CO;2-Q
F. Shih
Film-forming properties of plant proteins vary, depending on the protein's amino acid composition and molecular characteristics. Proteins from soy bean, wheat, and corn are readily available and films from these proteins have been investigated extensively. The proteins are normally dissolved or dispersed in suitable solvents. Then the resulting solutions or dispersions form free standing films either on an air-liquid interface by surface dehydration and heat-initiated polymerization or on a plate by casting the mixture and subsequent solvent evaporation. Various disulfide, hydrophobic, and hydrogen bonding interactions are involved in the film-forming mechanism which contribute to the development of film characteristics. Plant protein films in general are water sensitive and lack mechanical strength. However, they are good barriers against oxygen, and can be found in special applications as food products or edible food wrappers. Efforts are being made by modifications in processing conditions to improve the food-use functionality of the films. Future research to upgrade plant-protein films to be used packaging material is also discussed.
{"title":"Film‐forming properties and edible films of plant proteins","authors":"F. Shih","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<254::AID-FOOD254>3.3.CO;2-Q","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<254::AID-FOOD254>3.3.CO;2-Q","url":null,"abstract":"Film-forming properties of plant proteins vary, depending on the protein's amino acid composition and molecular characteristics. Proteins from soy bean, wheat, and corn are readily available and films from these proteins have been investigated extensively. The proteins are normally dissolved or dispersed in suitable solvents. Then the resulting solutions or dispersions form free standing films either on an air-liquid interface by surface dehydration and heat-initiated polymerization or on a plate by casting the mixture and subsequent solvent evaporation. Various disulfide, hydrophobic, and hydrogen bonding interactions are involved in the film-forming mechanism which contribute to the development of film characteristics. Plant protein films in general are water sensitive and lack mechanical strength. However, they are good barriers against oxygen, and can be found in special applications as food products or edible food wrappers. Efforts are being made by modifications in processing conditions to improve the food-use functionality of the films. Future research to upgrade plant-protein films to be used packaging material is also discussed.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"63 1","pages":"254-256"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80502167","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<217::AID-FOOD217>3.3.CO;2-U
M. Soral-Śmietana, A. Świgoń, R. Amarowicz, L. Sijtsma
{"title":"The solubility of trypsin pea protein hydrolysates","authors":"M. Soral-Śmietana, A. Świgoń, R. Amarowicz, L. Sijtsma","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<217::AID-FOOD217>3.3.CO;2-U","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<217::AID-FOOD217>3.3.CO;2-U","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"24 1","pages":"217-218"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78290948","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 : 1998-04-01DOI: 10.1002/(SICI)1521-3803(199804)42:02<75::AID-FOOD75>3.3.CO;2-6
B. Matthäus
HPLC has been applied for the analysis of neutral phenolic compounds in rapeseed. Extraction of phenolic compounds with 70% (v/v) methanol, separation of neutral and acidic phenolic compounds by solid phase extraction with a C 18 -cartridge and HPLC separation of the extracts so obtained are described. Additionally, a rapeseed extract was fractionated by a simple chromatographic method using Sephadex LH-20. Six main compounds from the extract were isolated. A further purification was performed by preparative HPLC and a C 18 -cartridge are used to isolate the neutral phenolic compounds. An attempt to identify the compounds was made from the UV-spectra corresponding to each isolated peak of the chromatogram.
{"title":"Isolation, fractionation and HPLC analysis of neutral phenolic compounds in rapeseeds","authors":"B. Matthäus","doi":"10.1002/(SICI)1521-3803(199804)42:02<75::AID-FOOD75>3.3.CO;2-6","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199804)42:02<75::AID-FOOD75>3.3.CO;2-6","url":null,"abstract":"HPLC has been applied for the analysis of neutral phenolic compounds in rapeseed. Extraction of phenolic compounds with 70% (v/v) methanol, separation of neutral and acidic phenolic compounds by solid phase extraction with a C 18 -cartridge and HPLC separation of the extracts so obtained are described. Additionally, a rapeseed extract was fractionated by a simple chromatographic method using Sephadex LH-20. Six main compounds from the extract were isolated. A further purification was performed by preparative HPLC and a C 18 -cartridge are used to isolate the neutral phenolic compounds. An attempt to identify the compounds was made from the UV-spectra corresponding to each isolated peak of the chromatogram.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"4 1","pages":"75-80"},"PeriodicalIF":0.0,"publicationDate":"1998-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86428324","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 : 1998-04-01DOI: 10.1002/(SICI)1521-3803(199804)42:02<71::AID-FOOD71>3.3.CO;2-U
S. Jood, S. Bishnoi, A. Sharma
Some high yielding cultivars of chickpea (Kabuli and desi) (Cicer arietinum) and lentil (Lens esculenta) were used for chemical analysis and physico-chemical properties namely protein, fat, sugars, starch, in vitro digestibility of starch and protein; seed weight, seed volume, seed density, hydration capacity, swelling capacity, water absorption capacity and cooking time. Among chickpea, Gora Hisari (Kabuli) and Haryana Chana (desi) cultivars, and among lentil LH 82-6 cultivar manifested higher contents of protein, fat, sugars, starch and in vitro digestibility of starch and protein. Values of seed volume, seed density, hydration capacity, swelling capacity and water absorption capacity were also found higher for these cultivars which might have contributed towards less cooking time.
{"title":"Chemical analysis and physico-chemical properties of chickpea and lentil cultivars","authors":"S. Jood, S. Bishnoi, A. Sharma","doi":"10.1002/(SICI)1521-3803(199804)42:02<71::AID-FOOD71>3.3.CO;2-U","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199804)42:02<71::AID-FOOD71>3.3.CO;2-U","url":null,"abstract":"Some high yielding cultivars of chickpea (Kabuli and desi) (Cicer arietinum) and lentil (Lens esculenta) were used for chemical analysis and physico-chemical properties namely protein, fat, sugars, starch, in vitro digestibility of starch and protein; seed weight, seed volume, seed density, hydration capacity, swelling capacity, water absorption capacity and cooking time. Among chickpea, Gora Hisari (Kabuli) and Haryana Chana (desi) cultivars, and among lentil LH 82-6 cultivar manifested higher contents of protein, fat, sugars, starch and in vitro digestibility of starch and protein. Values of seed volume, seed density, hydration capacity, swelling capacity and water absorption capacity were also found higher for these cultivars which might have contributed towards less cooking time.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"10 1","pages":"71-74"},"PeriodicalIF":0.0,"publicationDate":"1998-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76165848","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 : 1998-04-01DOI: 10.1002/(SICI)1521-3803(199804)42:02<84::AID-FOOD84>3.3.CO;2-A
E. Adeyeye
The flour from three colour cultivars of hulled and dehulled seeds of the African yam bean (AYB) (Sphenostylis stenocarpa) was analysed for anatomical fractions: proximate, mineral, fatty and amino acids composition. The seed hull varied between 8.25% and 9.14%. Na, K, Ca, Mn, Fe, Zn are preferably found in the hulled samples. Essential fatty acids as well as essential amino acids are more enriched in the hulled samples than in the endosperm. Correlation coefficient results showed that proximate composition (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), mineral composition (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), fatty acids (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), fatty acids saturation (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ) and amino acids (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ) were significant at α = 0.05 in the samples shown in parentheses with values having high positive correlation coefficients ranging from 0.82 to 1.00. These results showed that dehulling of African yam bean seeds will lead to reduction in the nutritional qualities of the AYB.
对非洲山药豆(AYB) (Sphenostylis stenocarpa)去壳和去壳种子的三种颜色品种的面粉进行了解剖学部分的分析:近似成分、矿物质、脂肪和氨基酸组成。种壳率在8.25% ~ 9.14%之间。Na, K, Ca, Mn, Fe, Zn主要存在于去壳样品中。必需脂肪酸和必需氨基酸在去壳样品中比在胚乳中更丰富。相关系数结果表明,近似成分(rD 1 D, 2、1 E 2,射频1 F 2),矿物成分(rD 1 D, 2、1 E 2,射频1 F 2),脂肪酸(rD 1 D, 2、1 E 2,射频1 F 2),脂肪酸饱和度(rD 1 D, 2、1 E 2,射频1 F 2)和氨基酸(rD 1 D, 2、1 E 2,射频1 F 2)是重要的在括号中所示的样品α= 0.05的值有较高的正相关系数从0.82到1.00不等。这些结果表明，非洲山药豆种子去皮会导致其营养品质下降。
{"title":"The relative merits of the presence of hull on the nutritional qualities of the African yam bean flour","authors":"E. Adeyeye","doi":"10.1002/(SICI)1521-3803(199804)42:02<84::AID-FOOD84>3.3.CO;2-A","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199804)42:02<84::AID-FOOD84>3.3.CO;2-A","url":null,"abstract":"The flour from three colour cultivars of hulled and dehulled seeds of the African yam bean (AYB) (Sphenostylis stenocarpa) was analysed for anatomical fractions: proximate, mineral, fatty and amino acids composition. The seed hull varied between 8.25% and 9.14%. Na, K, Ca, Mn, Fe, Zn are preferably found in the hulled samples. Essential fatty acids as well as essential amino acids are more enriched in the hulled samples than in the endosperm. Correlation coefficient results showed that proximate composition (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), mineral composition (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), fatty acids (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ), fatty acids saturation (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ) and amino acids (rD 1 D 2 , rE 1 E 2 , rF 1 F 2 ) were significant at α = 0.05 in the samples shown in parentheses with values having high positive correlation coefficients ranging from 0.82 to 1.00. These results showed that dehulling of African yam bean seeds will lead to reduction in the nutritional qualities of the AYB.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"25 1","pages":"84-88"},"PeriodicalIF":0.0,"publicationDate":"1998-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88226922","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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