Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<131::AID-FOOD131>3.3.CO;2-D
Soichiro Nakamura, S. Nakai
{"title":"Effects of proline substitution of the active site helix on dipeptide synthesis mediated by Bacillus stearothermophilus neutral protease","authors":"Soichiro Nakamura, S. Nakai","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<131::AID-FOOD131>3.3.CO;2-D","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<131::AID-FOOD131>3.3.CO;2-D","url":null,"abstract":"Effects of structural stabilization on dipeptide synthesis mediated by Bacillus stearothermophilus neutral protease was investigated. A proline residue was introduced into the N-terminus (I140P and D141P), the middle (L147P) and C-terminus (D153P) of the active site helix (G138-Y154) as reported by Nakamura et al. (1997). Mutants I140P and D141P were found to be 60 and 39-fold more stable than the wild-type enzyme in anhydrous dimethylformamide (DMF), respectively. The addition of DMF to the reaction medium markedly improved the efficiency of forming a sweet aspartyl dipeptide analog of aspartame, Z-L-Asp-Met-OMe, except L147P. Mutants I140P and D141P greatly promoted the synthesis in 60% DMF, in which the dipeptide yields were 3- and 2-times that of the wild type, respectively.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"99 1","pages":"131-134"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85774847","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<179::AID-FOOD179>3.3.CO;2-2
A. N. Danilenko, V. T. Dianova, E. E. Braudo, T. Henning, Ralf Mothes, K. Schwenke
{"title":"A novel approach to the evaluation of hydrophobicity of food proteins","authors":"A. N. Danilenko, V. T. Dianova, E. E. Braudo, T. Henning, Ralf Mothes, K. Schwenke","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<179::AID-FOOD179>3.3.CO;2-2","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<179::AID-FOOD179>3.3.CO;2-2","url":null,"abstract":"Different approaches used in the determination of surface hydrophobicity of proteins based on measurements of their partial heat capacity are discussed. They include the determination of the hydration heat capacity of a protein both in the unfolded and the native state and the determination of the increase in accessible to the solvent non-polar surface at the denaturation. The hydration heat capacity of a protein characterizes its net surface hydrophobicity or hydrophobic-hydrophilic balance. There was evaluated surface hydrophobicity of faba bean legumin and the product of its limited proteolysis with trypsin - legumin-T. It is shown that legumin-T in the native state has a higher hydration heat capacity and, hence, highcr net surfacc hydrophobicity than legumin, whereas hydration heat capacity of both proteins in the unfolded state does not differ significantly. The denaturation of legumin is accompanied by a grcater increase in accessible to the solvent non-polar surface than the denaturation of legumin-T. This differencc predetermines the higher conformational stability of legumin-T at temperatures below 310K compared to legumin.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"52 3 1","pages":"179-182"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84729435","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<266::AID-FOOD266>3.3.CO;2-E
D. Sessa, R. E. Wing
{"title":"Thermochemically‐modified soybean and corn protein products with enhanced metal‐binding properties","authors":"D. Sessa, R. E. Wing","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<266::AID-FOOD266>3.3.CO;2-E","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<266::AID-FOOD266>3.3.CO;2-E","url":null,"abstract":"Citric acid (CA), also known as 2-hydroxy- 1,2,3 propane tricarboxylic acid, was thermo-chemically reacted with food quality soy protein isolate (SPI), distillers' dried grains (DDG), produced from corn dry milling, and corn gluten meal (CGM), produced from corn wet milling, to generate acid-stable products with enhanced metal-binding properties. CA dehydrates at high temperature to form an anhydride that can interact with nucleophilic functional groups of protein or carbohydrate to generate ester or acyl derivatives. Effects of temperature, CA concentration, pH and reaction time were evaluated to show that SPI, DDG, and CGM, when heated in the range 1 10-120 °C with CA at 1 : 1 w/w ratio, under endogenous acidic conditions for 24 h. yielded reaction products with reaction efficiencies >60% which possessed 4.13, 4.19 and 4.26 mmol COOH/g, respectively. FTIR data of original heated protein compared with their respective CA products demonstrated additional absorbances indicative of ester and carboxyl linkages. The SPI/CA, DDG/CA, and CGM/CA products effectively bound 1.18, 1.07, and 0.98 mmol Cu 2+ /g, respectively, when analysed by ion plasma spectrometry. Solid state 27 Al NMR supported the metal binding characteristics of CA reaction products and demonstrated that Al 3+ was bound ionically to carboxyl groups present on the reaction product. Amino acid composition studies showed diminished amounts of amino acids with nucleophilic reactive groups in all three CA reaction products. The CA reaction products are highly resistant to acid hydrolysis with 6 N HCI for 4 h at 145°C. The biobased products generated in this study possess cation-exchange capability and potential biodegradability that may have an outlet for industrial wastewater treatment.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"7 1","pages":"266-268"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85236209","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<168::AID-FOOD168>3.3.CO;2-A
L. Kotova, N. Lapteva, I. Vaintraub
{"title":"An improved method of purification of protein deamidase from germinating seeds","authors":"L. Kotova, N. Lapteva, I. Vaintraub","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<168::AID-FOOD168>3.3.CO;2-A","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<168::AID-FOOD168>3.3.CO;2-A","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"51 1","pages":"168-169"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85579424","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<240::AID-FOOD240>3.3.CO;2-9
H. Saeki
{"title":"Functional changes in fish myofibrillar protein by conjugation with glucose and dextran","authors":"H. Saeki","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<240::AID-FOOD240>3.3.CO;2-9","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<240::AID-FOOD240>3.3.CO;2-9","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"70 1","pages":"240-241"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75317698","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<170::AID-FOOD170>3.3.CO;2-1
B. Schlesier, G. Koch, C. Horstmann
{"title":"Characterization of a class II chitinase from jack bean (Canavalia ensiformis) seeds","authors":"B. Schlesier, G. Koch, C. Horstmann","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<170::AID-FOOD170>3.3.CO;2-1","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<170::AID-FOOD170>3.3.CO;2-1","url":null,"abstract":"","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"22 1","pages":"170-170"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74783099","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<210::AID-FOOD210>3.3.CO;2-L
R. Lásztity, S. Tömösközi, E. Szilägyi, J. Gaugecz
{"title":"Modification of functional properties by rearrangement of disulfide bonds and change of ratio of protein fractions","authors":"R. Lásztity, S. Tömösközi, E. Szilägyi, J. Gaugecz","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<210::AID-FOOD210>3.3.CO;2-L","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<210::AID-FOOD210>3.3.CO;2-L","url":null,"abstract":"The growing use of different protein isolates (and concentrates) in food production in many cases requires modification of functional properties of isolates in order to assure the optimal physical (nutritional) properties of the endproduct. A number of possible ways of modification is known including chemical, physical procedures and also use of recombinant gene technology. Such technologies are in many cases expensive and are connected with food safety problems. In search for relatively cheap and safety process we studied the possibilities of applying rearrangement of disulfide bonds and change of ratio of protein fractions. The models used in experiments were: gluten-, soy-, pea-, and wheat germ proteins. It was found that gluten polypeptide mixtures of same composition reoxydized under different conditions were transformed to protein masses of quite different functional properties. The same procedure resulted in only slight changes in the case of reduction and reoxydation of legume- and wheat germ proteins. The study of some protein mixtures showed that the functional properties did not change linearly with the composition of the mixture. In many cases maxima of some parameters were observed.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"19 1","pages":"210-212"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84231361","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<264::AID-FOOD264>3.3.CO;2-M
C. Marquié, A. Tessier, C. Aymard, S. Guilbert
{"title":"How to monitor the protein cross‐linking by formaldehyde, glutaraldehyde or glyoxal in cotton‐seed protein‐based films?","authors":"C. Marquié, A. Tessier, C. Aymard, S. Guilbert","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<264::AID-FOOD264>3.3.CO;2-M","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<264::AID-FOOD264>3.3.CO;2-M","url":null,"abstract":"Protein cross-linking treatments by formaldehyde, glutaraldehyde and glyoxal are applied to enhance the maximum puncture force of films made with cottonseed flours. A sensitive and reproductible HPLC method to determine reactive lysine content of films was developped. The cross-linking of cottonseed proteins resulted in the decrease of reactive lysine content within the film. The maximum puncture force of the films is correlated with the modified reactive lysine content after cross-linking treatments. Of the three cross-linking agents, formaldehyde was the most effective to enhance the maximum puncture force of the films despite its moderate reaction with only 50% of reactive lysine in films. By contrast, glutaraldehyde which reacted with nearly 100% of lysine, led to less resistant films. The impact of protein cross-linking on maximum puncture force of films cannot be explained solely by the number of lysyl groups involved in the cross-linking reaction. It is also determined by the modification of intermolecular interactions between protein chains caused by a \"protein intemal plasticization effect\" due to the chemical modifications in protein structure after cross-linking treatments. (Resume d'auteur)","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"8 1","pages":"264-265"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83470869","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<160::AID-FOOD160>3.3.CO;2-5
T. Henning, S. Dudek, K. Schwenke, A. N. Danilenko, E. E. Braudo
{"title":"Limited tryptic hydrolysis of faba bean legumin: Conformational stability of legumin‐T","authors":"T. Henning, S. Dudek, K. Schwenke, A. N. Danilenko, E. E. Braudo","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<160::AID-FOOD160>3.3.CO;2-5","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<160::AID-FOOD160>3.3.CO;2-5","url":null,"abstract":"The conformational stability of legumin and legumin-T was evaluated by studying the equilibrium unfolding in the presence of guanidine hydrochloride. The obtained thermodynamic parameters for the folding/unfolding-reaction (conformational stability ΔG buffer o at 25 °C, its dependence on denaturant concentration m and the half denaturant concentration value [denaturant] 1/2 ) provided evidence that only a rather small decrease in the conformational stability of the legumin after modification to legumin-T occurs under these conditions.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"15 1","pages":"160-161"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75503283","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}
Nahrung-foodPub Date : 1998-08-01DOI: 10.1002/(SICI)1521-3803(199808)42:03/04<257::AID-FOOD257>3.3.CO;2-E
E. A. Podorozhko, E. Kurskaya, L. M. Andreeva
{"title":"Influence of the preliminary swelling of the dispersions of fibrous collagen on their ability of non‐covalent gel‐formation","authors":"E. A. Podorozhko, E. Kurskaya, L. M. Andreeva","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<257::AID-FOOD257>3.3.CO;2-E","DOIUrl":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<257::AID-FOOD257>3.3.CO;2-E","url":null,"abstract":"It was established that as a result of the maximum swelling (HCl, pH 3) the dispersed particles of fibrous collagen isolated from limed bovine derma irreversibly change their morphology. This results in changing the nature of supramolecular packing of protein - the transition of swollen bunches of fibrils into separate fibrils. Using method of adsorption of hydrophobic probe sodium dodecylsulphate it was found that under these conditions the significant increase in number of non-polar protein groups, able to participate in intermolecular interactions, took place. Subsequent lowering of the swelling capacity of the dispersed particles (from 19 to 2.2-2.5 g of tightly bound solvent per I g of dry collagen) resulted in the formation ofthe elastic macroisotropic gels. Hydrophobic nature of knots of gel network was confirmed by their stability in water until 62°C and destruction in concentrated solutions of urea and guanidine hydrochloride.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"316 1","pages":"257-259"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76457972","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}