Fractionation and characterisation for antioxidant activity of hydrolysed whey protein

Whey protein isolate (WPI) was hydrolysed for 1 h using Alcalase, Protamex and Flavourzyme. Native WPI, hydrolysed WPI and two commercial WPI hydrolysates were subjected to fractionation by size exclusion chromatography. Antioxidant activity of WPI fractions was measured with a liposome‐oxidising system (50 µM FeCl₃/0.1 µM ascorbate, pH 7.0). Lipid oxidation was measured as thiobarbituric acid‐reactive substances (TBARS). Gel electrophoresis and amino acid analysis were run to identify the peptide composition. The influence of amino acid composition on antioxidant activity was evaluated using multivariate analysis methods (correlation analysis, principal component analysis, multiple linear regression and discriminant analysis). TBARS assays indicated the presence of antioxidant activity in all protein fractions, including non‐hydrolysed WPI. For native and hydrolysed WPI samples the first fraction (> 45 kDa) showed a higher TBARS inhibition effect (24–27%) when compared with lower‐molecular‐weight fractions and hydrolysate mixtures. In contrast, for commercial WPI hydrolysates a higher inhibitory effect was found in most of the lower‐molecular‐weight fractions (30–55%). The ability of WPI fractions to delay lipid oxidation was found to be related to the prevalence of histidine and hydrophobic amino acids. Copyright © 2004 Society of Chemical Industry     

蚕蛹蛋白纤维染色性能的研究

由粘胶和蚕蛹蛋白混纺而成的蚕蛹蛋白纤维，采用双活性基活性染料染色，对染色工艺条件作了重点试验。结果表明，pH值和温度是最大的影响因素，该纤维适宜低温、pH值近中性条件下上染和碱性条件下固色。     

Effect of Flour Quality, Ascorbic Acid, and DATEM on Dough Rheological Parameters and Hearth Loaves Characteristics

ABSTRACT: The effects of protein quality, protein content, ascorbic acid, diacetyl tartaric acid ester of monoglyc-erides (DATEM), and their interactions on dough rheology and hearth bread properties were studied by size-exclusion fast protein liquid chromatography, Kieffer Dough & Gluten Extensibility Rig, and small-scale baking of hearth loaves. The effect of protein content was either positive or negative on hearth loaf characteristics, form ratio, and area, depending on the amount of the largest glutenin polymers in the flour. Ascorbic acid brought out the potential in the wheat flour known as protein quality. Ascorbic acid and DATEM strengthened the doughs and improved hearth bread characteristics.     

Enzymic and in sacco methods to estimate rumen degradation of food protein in cattle

BACKGROUND: Two factorial studies compared enzymic and in sacco methods to estimate degradation of ruminant foods. Enzyme degradation (in vitro = enzyme) was determined from the release of leucine‐equivalent amino acid (LA) crude protein (CP) from sunflower meal (SF), maize gluten meal (MG), distillers' dark grain (DG) and field beans (FB) after their separate incubations with Streptomyces griseus enzyme for 0–24 h. In sacco crude protein (CP) degradation of these foods was estimated during washing (0 h) and rumen incubations in fistulated cows for 2–24 h. The LA data were expressed as g LA per either kg of CP (LACP) or acid‐hydrolysable LA (HLA) of each food and compared with in sacco data. RESULTS: These methods showed comparable degradation with time (P < 0.01). The in sacco and HLA were greater than LACP for all foods except MG where in sacco value was either lower or equal to LACP depending upon the incubation time (P > 0.05 or P < 0.05). Conversely, HLA was significantly (P < 0.01) greater than LACP from 2 h onwards. At 0 h, in sacco values were significantly greater than those of enzyme for SF, DG and FB (P < 0.05) but not for MG. The foods differed significantly for degradation constants (a, b, c) in each method (P < 0.05). CONCLUSIONS: Despite variations between in sacco and enzyme estimates for different foods, the relationships between these estimates suggest that the HLA enzyme method has the potential to estimate food degradation. Copyright © 2007 Society of Chemical Industry     

Effect of temperature on recombinant protein production using the Bm5/Bm5.NPV expression system

A series of experiments have been conducted using a recombinant baculovirus/insect cell expression system (Bm5/Bm5.NPV.CAT) to establish the optimum temperature for both cell growth and virus infection. Bm5 cell growth was found to be limited at temperatures below 22°C and ceased completely at temperatures above 34°C. In the range between 24 and 28°C, final cell densities always reached 96% of the highest achievable viable cell density. The shortest population doubling time was obtained at 28°C. Overall, a consistent increase in metabolism with increasing temperatures was observed. During the infection/viral replication phase, an increase in the temperature from 25 to 31°C resulted in a faster decrease in viable cell density and an earlier production of chloramphenicol acetyltransferase (CAT). Furthermore, protein yield at temperatures above 28°C was significantly reduced. Overall, the best temperature for the infection phase for the Bm5/Bm5.NPV expression system was found to be 25°C when the cells are cultured in serum free media.     

Predictive modelling of the 3-D structure of interleukin-13

Several atomic structures are now available for the family ofhelical cytokines, which includes growth hormone as well asmany of the interleukins. Using structural information fromfive members of this family, two alternative models of interleukin(IL)-13 are proposed. IL-13 has biological properties similarto those of IL-4 and, like the other interleukins, is a potentiallyimportant pharmaceutical target. The model of IL-13 is discussedand compared with the known interleukin structures.     

磺化竹红菌素对蛋白质荧光猝灭机理的研究

本文详细研究了磺化竹红菌素对多种蛋白质在溶液状态下的荧光猝灭过程。结果表明，磺化竹红菌素对多种蛋白质荧光猝灭服从Ｓｔｅｎ－Ｖｏｌｍｅｒ曲线。实验观察了温度、粘度、ｐＨ值和盐酸胍对荧光猝灭过程的影响。由于磺化竹红菌素是一两性分子，对于不同蛋白具有不同猝灭过程；磺化竹红菌素对蛋白质的荧光猝灭常数Ｋｑ在１０＾１３ｍｏｌ／Ｌ．ｓ＾－１左右，这说明，磺化竹红菌素是一种比其它蛋白质荧光猝灭剂更加有效的荧光猝灭     

大豆蛋白分离工艺研究

阐述了大豆蛋白质的分离原理,分析了运用“碱提酸沉”分离法提取大豆蛋白质过程中,豆粕的粉碎方式、浸提温度、浸提时间、浸提液的pH值以及离心工艺对提取效果的影响,为大豆蛋白／聚丙烯腈纤维的工业化生产提供了依据。     

Modulation of the enzymatic activity of papain by interdomain residues remote from the active site

The two main catalytic residues Cys25 and Hisl59 of the monomericcysteine protease papain are located on different walls of acleft formed by two domains. This topology suggests a possiblerelationship between relative domain organization and catalyticmechanism. The effect on enzymatic parameters of structuralmodifications at various locations of the twodomain interfaceof papain was examined by individual or double replacementsby Ala of pairs of interacting residues. Most modificationshad no effect on enzyme activity. However, the enzyme's substrateturnover (k_cat) decreased following simultaneous alterationof the two most conserved residues, forming an apolar contactlocated 15 Å away from the active site. The pH activityprofile of the double mutant was unchanged, indicating a conservedionization state of the active site thiolate-imidazolium ionpair. This state is strongly dependent on the distance separatingthe two residues, thus suggesting that the active site geometryhas not been significantly altered. Efficient enzymatic activityin papain requires more than a correct active site geometryand is influenced by domain packing properties in a region remotefrom the active site.     

蛋白质分子链的超声速孤立子

在Ｄａｖｙｄｏｖ简谐蛋白质分子链模型的基础上，进行合理的连续近似处理，得到了超声速和亚声速孤立子解，并求得孤立子能量．