Influence of residual milk-clotting enzyme and proteolysis on melting properties of soft cheese

In this work, we assessed the influence of coagulant residual activity and primary proteolysis on Cremoso Argentino cheese melting properties. For that purpose, we made Cremoso soft cheeses using different amounts of coagulant, and also obtained samples in which milk-clotting enzyme was inactivated. Primary proteolysis correlated with residual activity of coagulant in early stages of cheese ripening; however, it was similar in all cheeses after 30 days. The hydrolysis of caseins did not significantly affect the melting ability of the cheeses, expressed as the area increase after heating samples under standardized conditions. Samples with similar proximate composition showed some changes in meltability; those seemed related to pH evolution during ripening.     

Influence of composition on the biochemical and sensory characteristics of commercial Cheddar cheese of variable quality and fat content

Ten commercial Cheddar cheeses of variable quality differing in fat content and age were subjected to compositional, proteolytic, lipolytic and sensory analyses. The compositional parameters of the full-fat cheeses were predominantly outside those typically associated with good-quality cheese. Sensory analysis discriminated the full-fat cheeses predominantly by age, with the longer ripened cheeses associated with more negative attributes, some which appeared to be due to excessive lipolysis and/or β-casein breakdown. Both proteolysis and lipolysis appear to be age dependent. The two reduced-fat cheeses were clearly discriminated from the eight full-fat cheeses by sensory analysis that appeared to be due to differences in composition and the extent of lipolysis.     

Physicochemical differences between Croatian cheese matured in a lamb skin sack (Sir iz misine) and cheese matured in a rind throughout ripening

The aim of this study was to research differences in physicochemical parameters between Croatian cheese in a lamb skin sack (Sir iz misine) and cheese in a rind throughout ripening. Cheese in a sack had significantly (P < 0.05) lower content of total solids, fat, proteins and salt which showed the ‘protective’ effect of skin sack and higher permeability of natural rind. The water‐soluble nitrogen in the total nitrogen (%TN) and 12% trichloroacetic acid‐soluble nitrogen (%TN) at the end of ripening was significantly (P < 0.05) higher in cheese in a sack than in cheese in a rind which indicates intensive proteolysis in cheese in a sack.     

Use of a new milk-clotting protease from Thermomucor indicae-seudaticae N31 as coagulant and changes during ripening of Prato cheese

Prato cheeses were manufactured using coagulant from Thermomucor indicae-seudaticae N31 or a commercial coagulant. Cheeses were characterised using the following analysis: yield; fat; acidity; moisture; ash; salt; pH; total nitrogen; total protein; NS-pH 4.6/NT*100; NS-TCA 12%/NT*100; casein electrophoresis; and RP-HPLC. The results were statistically analysed and revealed that the proteolytic indices were not significantly different throughout the 60 days of ripening of cheeses made with either coagulant. Even though there were some quantitative differences in the peptide profile of cheeses, the enzyme from T. indicae-seudaticae N31 was used in the production of good quality Prato cheese without having to change the established technological parameters of the process.     

Desmin and troponin T are degraded faster in type IIb muscle fibers than in type I fibers during postmortem aging of porcine muscle

A novel approach was applied in this study to directly evaluate the effect of muscle fiber type on postmortem protein degradation. Porcine muscle fibers were isolated from longissimus muscle at day 1, 3, and 6 postmortem. Fibers were sorted by immunochemical myosin heavy chain isoform typing. Western blot analysis of fibers pooled separately into type I or IIb showed that the relative amounts of 39- and 50-kDa desmin degradation fragments at day 6, and 28- to 31-kDa fragments of troponin T fast type isoform (fTnT) at day 1 and 6 postmortem were higher in type IIb than in type I fibers. At day 6 troponin T slow type isoform (sTnT) was less degraded than fTnT in type I fibers. These results indicated greater rate and extent of proteolysis in type IIb than in type I fibers and higher susceptibility of fTnT to proteolysis than that of sTnT isoform.     

Evidence against the non-enzymatic calcium theory of tenderization

The objective of the present study was to determine whether variation in the tenderization of lamb longissimus could be attributed to variations in the rise in free calcium postmortem and sarcomere lengthening post rigor. The longissimus muscle of 10 crossbred lambs (Romney×Coopworth) was sampled at 1 and 7 days postmortem for determination of MIRINZ shear force, myofibrillar fragmentation index (MFI), sarcomere length, free calcium, and proteolysis of troponin-T. Despite considerable variation in tenderness and tenderization of the muscles, sarcomere lengthening was not observed. The concentration of free calcium at 7 days postmortem correlated significantly with the MFI (r=0.640; P<0.05) and tended to correlate with the shear force (r=−0.596; P<0.1) and degradation of troponin-T (r=0.625; P<0.1). Degradation of troponin-T was significantly correlated with tenderization (r=0.664; P<0.05). Troponin-T is a calpain substrate, but reportedly is not degraded through a direct effect from calcium. The present results, therefore, suggest that the variation in free calcium in postmortem muscle affects tenderization through an effect on the calpain system and not through a direct effect of calcium on myofibrillar proteins. Consequently, the results of this study do not support the (calcium) theory that calcium directly affects tenderization.     

Secondary proteolysis in Serra cheese during ripening and throughout the cheese-making season

 Experimental Serra cheeses were manufactured from raw ewe’s milk and thistle flowers following a two-way factorial design. The content of nitrogen soluble in water (WSN), in 2% trichloroacetic acid (2% TCA-N), in 12% TCA (TCA-N) and in 5% phosphotungstic acid (5% PTA-N), and the pH and salt-in-moisture concentration were measured throughout the ripening period (sampling at 0, 7, 21 and 35 days) and the cheese-making season (sampling in November, February and May). Proteolysis in 35-day-old Serra cheese was quantitatively high [average values of 34.6% and 11.9% for WSN/TN (total nitrogen) and 2% TCA-N/TN, respectively], but qualitatively low (average values of 5.8% and 1.2% for 12% TCA-N/TN and 5% PTA-N/TN, respectively). The ratios WSN/TN and 2% TCA-N/TN were lowest for cheeses ripened in February, whereas the ratio 12% TCA-N/TN was highest for cheeses ripened in November. By 35 days of ripening, the average pH and salt-in-moisture concentration values were 5.2 and 4.8%, respectively. No correlation was found to occur between the measured pH or salt-in-moisture concentration and the values of soluble nitrogen fractions throughout the cheese-making season. Received: 14 February 1996/Revised version: 4 June 1996     

Effect of processing conditions on proteolysis and taste of dry-cured sausages

 This paper deals with the influence of industrial practices such as use of starters (Lactobacillus sake and Staphylococcus carnosus), preripening (3 days at 5°C) and drying temperatures (8 and 16°C) on proteolysis, ammonia production and the taste of “salchichón”, a traditional Spanish dry-cured sausage lacking surface mould. pH dropped more sharply in the presence of a starter and at a high drying temperature (16°C); preripening did not affect the pH. The highest value for non-protein nitrogen (NPN), 16% of total nitrogen, was observed to occur in samples with the lowest pH (4.7–4.8). Total volatile basic nitrogen (TVBN) increased during drying due to the deaminase activity of internal microbial flora, which was not great (0.5–1.0% of total nitrogen) enough to affect the pH, and significantly in samples showing a larger decrease of pH. The greater proteolysis in samples with starter did not affect the assessors’ taste preference. Assessors clearly preferred those samples without starter that were dried at low temperature (8°C); however, samples with starter showed excellent commercial appearance since they dried more homogeneously. An equilibrium point must be found between acid production and taste. Received: 12 February 1996/Revised version: 24 May 1996     

Tissue degradation,amino acid liberation and bacterial decomposition of bulk stored capelin

Bulk stored capelin with high contents of feed in the gut is easily solubilised because of high proteolytic activity. The amino acids most quickly liberated are arginine, serine, histidine, leucine, lysine and tyrosine; glycine, aspartic acid and glutamic acid are liberated at a slower rate. Bacterial activity results in a rapid and considerable decrease in total amounts of tyrosine, lysine, serine, arginine and histidine. The main products formed by bacterial decomposition of lysine, histidine and arginine are cadaverine, histamine and putrescine, respectively. Storage of capelin in the presence of antibiotics increased the amounts of free amino acids and total amino acids. After 10 days' storage at 6°C, about 30% of the total amino acid content in fish treated with antibiotics were fee amino acids.     

Relationship between proteolysis and angiotensin-I-converting enzyme inhibition in different cheeses

The inhibition of angiotensin-I-converting enzyme (ACE) by the ethanol (70%)-soluble fraction (ESF) from different cheeses was analysed with an extract from rabbit lung acetone powder as enzyme source and 2-furanacryloyl-1-phenylalanylglycylglycine (FAPGG) as substrate. Proteolysis was assessed by a spectroscopic o-phthaldialdehyde (OPA) assay of the pH 4.6-soluble fraction and ESF. Peptides in the ESF were separated by reverse phase-HPLC. The traditional Norwegian cheese Gamalost had per unit cheese weight higher ACE inhibition potential than Brie, Roquefort and Gouda-type cheese, likely due to the combination of highest protein content and most extensive proteolysis providing a high content of ACE inhibitory peptides. However, ACE-inhibition expressed as IC₅₀ per unit peptide concentration from ESF assessed by the OPA-assay was highest for Kesam, a Quark-type cheese with a low degree of proteolysis.