Characterisation and durability of contemporary unsized Xuan paper

In China, Xuan paper has been the paper of choice as artwork support and for conservation, for several centuries. However, little is known about its material properties, especially given the many grades of sized and unsized Xuan paper. In addition, there is a lack of information on its degradation. In this research, a selection of contemporary unsized Xuan papers was investigated, representing diverse raw materials. Seven out of twelve contemporary unsized Xuan papers were determined to be approximately neutral and contain > 2% alkaline reserve, indicating good durability. Viscometry was used to determine the degree of polymerisation (DP) as none of the samples gave significant reactions to the phloroglucinol spot test. The average DP of ten contemporary unsized Xuan papers is ~ 1700, excluding two papers that have presumably been sun-bleached, and that exhibit significantly lower DP. Using X-ray fluorescence, it can be demonstrated that Ca and Si are the dominant elements and interestingly, Ca content is directly correlated with ash content and with alkaline reserve. Accelerated degradation was performed at two sets of environmental conditions, i.e. 90 °C, 30% RH and 60 °C, 70% RH, and the established degradation rates agreed with the Collections Demography model of paper degradation meaning that degradation of Xuan papers proceeds in the same way as other types of paper. This research gives fundamental insights into contemporary unsized Xuan papers, which exhibit good stability during accelerated degradation despite the low starting DP in the context of the samples used in this study. Our findings may inform methods of Xuan paper production, selection of Xuan paper for conservation purposes, as well as preventive conservation of Xuan paper-based artefacts.

Enterocin HZ produced by a wildEnterococcus faeciumstrain isolated from a traditional, starter-free pickled cheese

BacteriogenicEnterococcus faeciumHZ was identified by using biochemical (Strep-API 20, API-50 CHL, fatty acid profile) and 16S rRNA analysis (99·99 %).Ent. faeciumHZ was sensitive to clinically important antibiotics such as vancomycin, and did not have gelatinase and haemolysis activities. Enterocin HZ, a bacteriocin fromEnt. faeciumHZ, was sensitive to papain and tyripsin, but resistant to pepsin, lipase, catalase, α-amylase, organic solvents, detergents, ß-mercaptoethanol, and heat treatment (90 °C/30 min). It was biologically active at pH 2·0–9·0 and synthesised at the highest level in MRS or M17 broth at 32 or 37 °C with an inoculum amount of 0·1–0·5 % and an initial pH of 6·0–7·0. Enterocin HZ production reached maximum level at middle and late logarithmic phase and its molecular weight was ∼4·5 kDa. It was active against some Gram-positive foodborne bacteria.Ent. faeciumHZ or its bacteriocin enterocin HZ is a good candidate to be studied as a food biopreservative since enterocin HZ showed strong bactericidal activity againstListeria monocytogenesin UHT milk and alsoEnt. faeciumHZ grew very well in milk and produced enterocin HZ at maximum level.

Effect of protein concentration, pH, lactose content and pasteurization on thermal gelation of acid caprine whey protein concentrates

The influence of pH (4·5–6·5), sodium chloride content (125–375 mM), calcium chloride content (10–30 mM), protein concentration (70–90 g/l) and lactose content on the gel hardness of goat whey protein concentrate (GWPC) in relation to the origin of the acid whey (raw or pasteurized milk) was studied using a factorial design. Gels were obtained after heat treatment (90 °C, 30 min). Gel hardness was measured using texture analyser. Only protein concentration and pH were found to have a statistically significant effect on the gel hardness. An increase in the protein concentration resulted in an increase in the gel hardness. GWPC containing 800 g/kg protein formed gels with a hardness maximum at the pHi, whereas GWPC containing 300 g/kg protein did not form true gels. Whey from pasteurized milk formed softer gels than whey from raw milk. A high lactose content (≈360 g/kg) also reduced the gelation performance of GWPC.

Manejo do nitrogênio no milho em sucessão a plantas de cobertura de solo, sob plantio direto

Estabelecida a hipótese de que a antecipação da adubação nitrogenada promove acréscimo no rendimento de grãos de milho pela maior disponibilidade de N nos estádios iniciais de desenvolvimento, foi realizado um trabalho com o objetivo de avaliar diferentes manejos de N para o milho cultivado em sucessão a plantas de cobertura de solo. O experimento foi desenvolvido em área do Departamento de Solos da Universidade Federal de Santa Maria (RS), nos anos agrícolas de 1996/97, 1997/98 e 1998/99, em Argissolo Vermelho distrófico arênico (Hapludalf). O delineamento experimental foi de blocos ao acaso com parcelas subdivididas e três repetições. Nas parcelas principais (25 x 5 m), foram cultivadas três espécies para cobertura de solo no inverno: aveia preta (Avena strigosa Schieb), aveia preta + ervilhaca (Vicia sativa L.) e nabo forrageiro (Raphanus sativus). Nas subparcelas (5 x 5 m), aplicou-se N para o milho da seguinte maneira: (a) 00-00-00, (b) 00-30-90, (c) 30-30-60, (d) 60-30-30 e (e) 90-30-00, cuja seqüência para cada tratamento corresponde à quantidade de N em kg ha-1 aplicado em pré-semeadura-semeadura-cobertura do milho. A aplicação de N em pré-semeadura foi realizada após o manejo das plantas de cobertura de solo no inverno, enquanto em cobertura o N foi aplicado quando as plantas de milho estavam com quatro a seis folhas desenroladas. Utilizou-se uréia como fonte de N. Segundo os resultados, o milho cultivado em sucessão ao consórcio com aveia preta + ervilhaca mostrou melhor desempenho do que quando cultivado sobre resíduos de aveia preta e nabo forrageiro. A aplicação de N em pré-semeadura do milho é uma atitude de risco, sendo mais segura a aplicação de N na semeadura e em cobertura.

Potassium iodate-induced proteolysis in ultra heat treated milk during storage: the role of β-lactoglobulin and plasmin

SummaryThe report that addition of KI03 (0·1 mm) to milk before ultra high temperature (UHT) treatment induces extensive proteolysis during subsequent storage at 37 °C was confirmed. None was produced by addition of H202 KMn04 or K2Cr207. The pH optimum for KI03-induced proteolysis was between 7·0 and 8·0 and the temperature optimum 37—45 °C. β-Casein was particularly susceptible and the proteolysis pattern was similar to that caused by indigenous alkaline milk proteinase (MPA, plasmin). Addition of plasmin to milk before UHT treatment (140 °C/10 s) caused slight proteolysis during subsequent storage but addition of 0·1 mm-KI03 and plasmin caused extensive proteolysis which was prevented by addition of soyabean trypsin inhibitor, indicating the probable involvement of plasmin in KI03-induced proteolysis in UHT-treated milk. Equally extensive proteolysis occurred in serum protein-free casein micelle systems (SPFCM), with or without KI03, during storage at 37 °C following UHT treatment, indicating a role for whey proteins in KI03-induced proteolysis. Addition of β-lactoglobulin (β-lg) to a SPFCM system inhibited proteolysis, but extensive proteolysis occurred in a SPFCM system containing both β-lg and KI03. MPA-free Na caseinate (prepared by heating at 140 °C for 7 min) underwent extensive proteolysis when treated with plasmin before UHT treatment; proteolysis was inhibited by addition of °-lg to this system and KI03 reversed the inhibitory effect of β-lg. Plasmin proteolysis of isolated αs1-casein was inhibited by denatured β-lg (90 °C/30 min) at a level of 4 mg/ml but not by native β-lg. When denatured in the presence of KI03, β-lg had a lower free SH content than the control and was less inhibitory for plasmin in proteolysis of isolated αsl-casein. The results show that denatured β-lg inhibits plasmin proteolysis of caseins in UHT milk and that inhibition is prevented by KI03. This inhibition may occur via thiol–disulphide interchange, which is prevented if the SH group of ²-lg is oxidized by KI03, thus permitting the stimulatory effect of KI03 on proteolysis in UHT-treated milk.

The determination of the zeta potential of casein micelles

SUMMARYThe principle of moving boundary electrophoresis has been employed for the measurement of the electrophoretic mobility and subsequent calculation of zeta potential of bovine casein micelles. The zeta potential of casein micelles was observed to increase with increase in temperature (from 10 to 50 °C) and to decrease with decrease in pH. Heat treatment of milk between 90 °C/30 min and 135 °C/50 min had no significant effect on zeta potential. The zeta potential of casein micelles during rennet action decreases until all the κ-casein has been cleaved by the enzyme.The results of this study indicate that electrostatic interactions alone are not sufficient for an understanding of the absolute stability of casein micelles.