The addition of potassium iodate to milk at 0·1 mm before UHT treatment resulted in rapid breakdown of αs- and β-casein during subsequent aseptic storage. Maximum rates of proteolysis were observed at storage temperatures of 37–45 °C, but the reaction was strongly inhibited by storage at 55 °C and by increased holding time at 140 °C during the UHT sterilization. Iodate-induced proteolysis of purified αs1-and β-casein was detected only with solutions in the serum phase of raw milk; no proteolysis occurred with solutions in 01·M-phosphate buffer (pH 6·7) or in milk ultrafiltrate, irrespective of whether whey proteins and lactose were also added. Thus, it appears that iodate increased the activity of one or more proteolytic components which were present in milk and were unable to pass through an ultrafiltration membrane. However, it is unlikely that iodate acts by increasing the activity of proteinases produced by contaminant bacteria; the presence of iodate did not affect the activity of a proteolytic enzyme isolated from Pseudomonas fluorescens PM-1. Furthermore, iodate promoted protein breakdown during storage of milk drawn aseptically from the cow and subsequently UHT processed. It is suggested that iodate increased the activity of native milk proteinases, other than plasmin which was inactivated by UHT treatment, possibly by preventing thiol-disulphide exchange reactions during the heating process.

Carbonyl sulphide (COS) was detected in the headspace of Cheddar cheeses in concentrations ranging from 0·01 ng ml-1 to 0.3 ng ml-1. It was also found in the headspace above certain packaging materials and sealing materials used in the analytical procedures. Evidence that COS was produced within the cheese was given by the findings that experimental cheese containing added cysteine had consistently higher COS levels (up to 1·0 ng ml-1) and that COS could be produced chemically from mixtures of cysteine or methionine with riboflavin and ascorbic acid in laboratory trials.

As determined by the standard subjective assay procedure, the minimum in the heat stability–pH curve of milk persisted down to at least 116 °C. However when samples were not agitated during heating the minimum became progressively less pronounced as the assay temperature was lowered and it disappeared at approximately 116 °C. Activation energies (Ea) for unagitated samples were approximately 30 Kcal/mole at pH 6·87 (maximum) and at pH 7·18, throughout the temperature range 116–145 °C and for the pH 6·95 (minimum) sample at 116–125 °C; however Eα for the pH 6.95 sample increased to approximately 100 Kcal/mole in the range 127–135 °C suggesting that some highly temperature-dependent reaction had occurred and caused premature coagulation at certain pH values, i.e. to a heat stability minimum. The stability of concentrated milk (20% total solids) was very low at pH values above 6·9, regardless of whether the samples were agitated or not during heating and the maximum/minimum in the heat stability–pH curve persisted down to at least 90 °C in both agitated and quiescent samples.

Pickled soft cheese was made from recombined milk (30 % total solids, 8 % fat) containing buttermilk powder (0–4%) and stored in the pickle at room temperature (25±5 °C) for 135 d. The yield, quality and composition of cheese were followed periodically during storage. The addition of buttermilk slightly increased the yield and improved the flavour intensity of the cheese, whilst only slightly affecting its chemical composition.

The hydrolysis of isolated αs1- and β-caseins by Penicillium roqueforti aspartyl proteinase produced comparable quantities of pH 4·6 soluble N. The amount of non-protein nitrogen obtained with β-casein was clearly lower than that obtained with αs1-casein, showing that few low molecular weight peptides were released when this casein was hydrolysed. Electrophoresis of αs1-casein hydrolysates produced by aspartyl proteinase showed 5 bands of mobility close to or higher than that of αs1-casein. β-Casein hydrolysates gave 4 bands, 2 of which (βPrapl and βPrap2) showed low electrophoretic mobility. The products corresponding to βPrapl and βPrap2 were purified from a β-casein hydrolysate and identified as fragments Val98-Val209 and Glu100-Val209 of β-casein respectively. The occurrence of the βPrapl and βPrap2 bands in electrophoretic patterns obtained from sterile curd with aspartyl proteinase and controlled-flora curd, where P. roqueforti was the only micro-organism developing, showed the presence of aspartyl proteinase synthesis and activity in cheese. A band of very low electrophoretic mobility (βPrmpl) was present in electrophoregrams of controlled-flora curd inoculated with P. roqueforti. This band, resulting from the action of the metalloproteinase on β-casein, revealed that this enzyme was both synthesized in and active in cheese.

Eight samples of milk fat were selected for softening point (SP) range. They were separated into high, medium and low molecular weight triglyceride fractions by silicic acid-column chromatography to enable further separation into triglyceride classes by silver ion adsorption thin-layer chromatography. Correlation between triglyceride class content and SP was low. The molecular species composition of the triglyceride classes was determined and correlated with SP. The best correlations were between SP and some low and some high molecular weight triglycerides of the total fat and the trisaturated (SSS) triglyceride class. Correlation coefficients were determined between SP and mole percentage of individual fatty acids and groups of acids. The highest correlations were between SP and individual short chain-length fatty acids (C4–C10) and groupings of short chain-length acids (C4–C10) and groupings of long chain-length acids (C16–C20). The triglyceride class composition of a sample of milk fat was determined before and after interesterification. Interesterification increased the SP from 31·6 to 36·3 °C and produced increased amounts of both low and high and decreased amounts of medium molecular weight triglyceride molecular species in all triglyceride classes. The increases in the amounts of high molecular weight triglycerides were several times greater than the increase in the amounts of low molecular weight triglycerides.

Milks were prepared at 1·7- to 4-fold the initial concentration by combining skim-milk concentrated by ultrafiltration with cream, and used for Cheddar cheese-making. Starter growth was unaffected, but the increased buffering capacity in the more concentrated milks resulted in a slower decline in pH and a higher pH value in the cheese. Curd formation was faster despite the use of reduced amounts of rennet. With milk concentrated more than 2-fold, large amounts of fat were lost in the whey, so that the cheeses had less fat than normally. Fat losses may be partly related to the lower degree of aggregation of the casein micelles when the curd was cut. As the concentration factor of the milk increased, the rate of casein breakdown, the intensity of Cheddar flavour, and the levels of H2S and methanethiol in the cheese decreased. These factors may relate to the reduced concentration of active rennet retained in the curd at pressing.

Four enzymes of citrate metabolism (viz. citrate lyase, acetolactate synthase, diacetyl reductase and acetoin reductase) were constitutively present in cells of several strains of Streptococcus lactis subsp. diacetylactis. In strain DRC1, which was studied in detail, diacetyl reductase and acetoin reductase were partly repressed and acetolactate synthase partly induced by growth on citrate. The stage of growth also affected the formation of each enzyme. The buffer species affected the activity of acetolactate synthase, diacetyl reductase and acetoin reductase.

Citrate stimulated growth, totally induced citrate lyase, partly induced acetolactate synthase activity and partly repressed both diacetyl and acetoin reductases in Leuconostoc lactis NCW1. Similar results were obtained with 2 other leuconostocs and a heterofermentative lactobacillus. In 2 of the 3 leuconostocs tested, diacetyl reductase and acetoin reductase were NADPH specific, while in the 2 heterofermentative lactobacilli, they were NADH specific.

Samples of curd and cheese, taken throughout cheese-making with milks concentrated to different extents, were examined by light microscopy and by scanning and transmission electron microscopy. The mature cheeses were analysed for textural parameters by instrumental and sensory means. The protein was packed in larger, more compact areas and the fat was more segregated in the curds and cheeses from the more concentrated milks. The protein network increased in coarseness in proportion to the concentration factor of the milk, the relative differences being the same throughout cheese-making into the mature cheese. Thus, the basic structure of the protein network was laid down during the curd firming process and was not fundamentally altered later in cheese-making. The fat/protein interfaeial area in the cheese and the changes in structure during maturation decreased as the concentration factor of the milk increased. The instrumental firmness, cohesiveness and force and compression required to cause fracture, and the sensory firmness, crumbliness, granularity and dryness of the cheese all increased as the concentration factor of the milk increased. The adhesiveness declined and there was little change in elasticity, with increase in milk concentration factor. The textural differences were related to the smaller fat content, lower level of proteolysis, stronger links in the protein matrix and reduced capacity of the fat and protein phases to move relative to each other in the cheeses from the more concentrated milks.

Soluble extracts of 20 strains of thermophilic lactobacilli (Lactobacillus helveticus, L. lactis and L. bulgaricus) were prepared and added to milk for the culture of 10 strains of Streptococcus thermophilus. Acid production was stimulated in 64·5% of cases for 9 of these 10 strains. The L. helveticus extracts were the most stimulatory, but the same extracts did not always strongly stimulate each strain of Str. thermophilus. The stimulatory effects observed varied with the volume of extract and the strain of Str. thermophilus. The exception was Str. thermophilus 385, which was never stimulated. The stimulatory effects observed were due to aminopeptidases present in the lactobacillus extracts and were not related to a general caseinolytic activity. The possible addition of such extracts to milk for cooked hard cheese is discussed.

Cheese whey was used as substrate for submerged cultivation of 8 strains of 6 species of edible mushrooms (morel mushroom): Morchella crassipes (3 strains), M. angusticeps, M. rotunda, M. deliciosa, M. esculenta and an unidentified Morchella sp. Best growth of morel mushroom mycelium was obtained with one of the M. crassipes strains. The optimum growth conditions for the selected mycelium were as follows: initial pH, ~ 5·0–5·5; temperature, 25–28°C; inoculum size, 150–250 mg mycelium/100 ml whey; N sources: peptone and yeast extract; trace elements: K and Fe. More than 20 g/l mycelium was harvested in the form of pellets. Some growth kinetics studies were also performed. The initial carbohydrate (lactose) content was reduced from 5 to 0·4% at the end of the cultivation period. The specific growth rate of M. crassipes ATCC 13227 was from 1.0 to 6·4 x 10–2, depending on the growth phase. The harvested biomass contained about 45% protein, 5% fat and 8·5% ash (on a dry-weight basis). Essential amino acid content was comparable to the FAO standard, except for methionine, and unsaturated fatty acids predominated in the fat. The results with whey are compared with previously reported data on morel mushroom mycelium growth on waste sulphite liquors.