Microbial Non-Coagulant Enzymes Used in Cheese Making

2018 ◽  
pp. 204-221
Author(s):  
Ekaterini Moschopoulou
Keyword(s):  
Cross Linking ◽  
Peptide Bonds ◽  
Cheese Making ◽  
Cheese Ripening ◽  
Cheese Texture ◽  
Cheese Flavor ◽  
Flavor Development ◽  
Microbial Lipases ◽  
Bacteria And Fungi ◽  
Almost All

In this chapter, the use of microbial non-coagulant proteases, microbial lipases, and microbial transglutaminase in the cheese making procedure is discussed. Microbial proteases and lipases have been used for over 30 years to accelerate cheese ripening and consequently to enhance the cheese flavor development by increasing proteolysis and lipolysis level in a shorter time. They are commercially produced by bacteria and fungi species. Transglutaminase is a relative new enzyme, which catalyzes the cross-linking of peptide bonds and helps to improve the cheese texture and to increase the cheese yield. Today, cheeses from almost all cheese categories are produced using these enzymes.

scholarly journals Omics Approaches to Assess Flavor Development in Cheese

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 188
Author(s):  
Rania Anastasiou ◽  
Maria Kazou ◽  
Marina Georgalaki ◽  
Anastasios Aktypis ◽  
Georgia Zoumpopoulou ◽  
...  
Keyword(s):  
Amplicon Sequencing ◽  
Vital Role ◽  
Organoleptic Properties ◽  
Accurate Identification ◽  
Cheese Ripening ◽  
Sequencing Technologies ◽  
Cheese Flavor ◽  
Flavor Development ◽  
High Throughput Dna Sequencing ◽  
Integration Analysis

Cheese is characterized by a rich and complex microbiota that plays a vital role during both production and ripening, contributing significantly to the safety, quality, and sensory characteristics of the final product. In this context, it is vital to explore the microbiota composition and understand its dynamics and evolution during cheese manufacturing and ripening. Application of high-throughput DNA sequencing technologies have facilitated the more accurate identification of the cheese microbiome, detailed study of its potential functionality, and its contribution to the development of specific organoleptic properties. These technologies include amplicon sequencing, whole-metagenome shotgun sequencing, metatranscriptomics, and, most recently, metabolomics. In recent years, however, the application of multiple meta-omics approaches along with data integration analysis, which was enabled by advanced computational and bioinformatics tools, paved the way to better comprehension of the cheese ripening process, revealing significant associations between the cheese microbiota and metabolites, as well as their impact on cheese flavor and quality.

Accelerated cheese ripening: a method for increasing the number of lactic starter bacteria in cheese without detrimental effect to the cheese-making process, and its effect on the cheese ripening

1975 ◽  
Vol 42 (2) ◽  
pp. 313-326 ◽  
Author(s):  
H.-E. Pettersson ◽  
G. Sjöström
Keyword(s):  
Heat Treatment ◽  
Adverse Effect ◽  
Trichloroacetic Acid ◽  
Detrimental Effect ◽  
Phosphotungstic Acid ◽  
Cheese Making ◽  
Cheese Ripening ◽  
Constant Ph ◽  
Cheese Curd ◽  
Number Of Cells

SummaryA method is outlined for accelerating ripening in Swedish semihard cheese by increasing the number of lactic starter bacteria present in the cheese without impairing characteristic texture and flavour. In addition to the normal starter inoculum, suitable lactic starter bacteria whose lactic-acid-producing activity had been greatly reduced by previous sublethal heat treatment, were added to the cheesemilk. When suspensions of streptococci and lactobacilli cultivated at a constant pH were heated at 59 and 69°C respectively acid production was retarded by 5–10 h, which was found to be sufficient for the cheese-making. Proteolysis was lowered only 10–30% by these heating temperatures. Bacterial cell suspensions, prepared by the methods outlined and added to the cheesemilk, were incorporated in cheese curd to extents depending on the amount added and the type of starter. The number in the final cheese could be increased to a maximum of 4–5 times that of control cheese. No adverse effect of the extra starter bacteria on pH, fat content and water content of cheeses 24-h old was observed. Proteolysis, measured as the increase in trichloroacetic acid and phosphotungstic acid (PTA)-soluble N, increased with increasing number of cells in the cheese. Organoleptic judgements showed a positive correlation (r= 0·81) between taste and PTA-soluble N, which in turn was influenced by the number of cells in the final cheeses.

scholarly journals Food protein: Food colour interactions and its application in rapid protein assay

2010 ◽  
Vol 28 (No. 6) ◽  
pp. 506-513 ◽  
Author(s):  
M.G. Saeed S ◽  
S.U. Abdullah ◽  
S.A. Sayeed ◽  
R. Ali
Keyword(s):  
Food Systems ◽  
Binding Capacity ◽  
Food Protein ◽  
Food Proteins ◽  
Protein Food ◽  
Peptide Bonds ◽  
Protein Assay ◽  
Food Dye ◽  
Almost All

The uniform distribution of colours as additives in a majority of the food systems is a reliable indication that one or more components of foods are able to bind with colour molecules and act as their carriers. However, the food components acting as the colour carriers have not been identified. The present paper describes the binding capacity of Carmoisine with a variety of food proteins, our results have shown that the intensity, staining, and sharpness of the stained protein bands were excellent as compared to Coomassie Brilliant Blue-R-250, which is an established staining agent for visualising electrophoretically resolved proteins. The data illustrates that Carmoisine is a fast reacting dye forming colour-complexes with all types of food proteins including curry leaves proteins. The protein bands are visualised within an hour which is useful for the initial immediate protein identifications. The experiments related to the staining of the resolved proteins with Carmoisine have shown that the dye is highly sensitive, rapid, and lasting. The food-dye can provide a quick protein assay as often desired in research works, the results may be later confirmed by using Coomassie if so required. In view of its strong binding with almost all proteins, it was thought that human proteases present in the digestive tract may not hydrolyse the bound proteins completely and may restrict the proteolytic digestion. However, the experiments based on the tryptic digestibility in vitro revealed that colour binding has no adverse effect on hydrolysis of peptide bonds by the intestinal proteases.

scholarly journals Source of Enterococci in a Farmhouse Raw-Milk Cheese

2002 ◽  
Vol 68 (7) ◽  
pp. 3560-3565 ◽  
Author(s):  
R. Gelsomino ◽  
M. Vancanneyt ◽  
T. M. Cogan ◽  
S. Condon ◽  
J. Swings
Keyword(s):  
Raw Milk ◽  
Streptococcus Bovis ◽  
Human Feces ◽  
Natural Habitats ◽  
Enterococcus Casseliflavus ◽  
Flavor Development ◽  
Bulk Tank ◽  
Milking Machine ◽  
Raw Milk Cheese ◽  
Almost All

ABSTRACT Enterococci are widely distributed in raw-milk cheeses and are generally thought to positively affect flavor development. Their natural habitats are the human and animal intestinal tracts, but they are also found in soil, on plants, and in the intestines of insects and birds. The source of enterococci in raw-milk cheese is unknown. In the present study, an epidemiological approach with pulsed-field gel electrophoresis (PFGE) was used to type 646 Enterococcus strains which were isolated from a Cheddar-type cheese, the milk it was made from, the feces of cows and humans associated with the cheese-making unit, and the environment, including the milking equipment, the water used on the farm, and the cows' teats. Nine different PFGE patterns, three of Enterococcus casseliflavus, five of Enterococcus faecalis, and one of Enterococcus durans, were found. The same three clones, one of E. faecalis and two of E. casseliflavus, dominated almost all of the milk, cheese, and human fecal samples. The two E. casseliflavus clones were also found in the bulk tank and the milking machine even after chlorination, suggesting that a niche where enterococci could grow was present and that contamination with enterococci begins with the milking equipment. It is likely but unproven that the enterococci present in the human feces are due to consumption of the cheese. Cow feces were not considered the source of enterococci in the cheese, as Enterococcus faecium and Streptococcus bovis, which largely dominated the cows' intestinal tracts, were not found in either the milk or the cheese.

Assessment of swine, bovine and chicken pepsins as rennet substitutes for Cheddar cheese-making

1972 ◽  
Vol 39 (2) ◽  
pp. 261-273 ◽  
Author(s):  
Margaret L. Green
Keyword(s):  
Cheddar Cheese ◽  
Cheese Making ◽  
Stomach Mucosa ◽  
Milk Clotting ◽  
Cheese Ripening ◽  
Cheese Flavour ◽  
The Cost ◽  
Substrate Ph ◽  
Milk Clotting Activity

SummaryThree enzymes were assessed as rennet substitutes for cheese-making. The bovine and chicken pepsins used were relatively crude extracts of bovine stomach mucosa and chicken proventriculae respectively; the swine pepsin was a partially purified commercial product. The ratios of milk-clotting activity to general proteolytic activity were high for rennet and bovine pepsin and low for swine and chicken pepsins. Both bovine mucosa and chicken stomach gave low milk-clotting activities compared with calf stomach. For all the enzymes the chemical reactions causing milk clotting appeared to be the same. The milk-clotting activity showed a decrease with increase in substrate pH for all the enzymes, although they were all still active at pH 6·81.Duplicate cheeses were made from each of the swine, bovine and chicken pepsins, with rennet as a standard in each trial. The cheese-making process was similar with each enzyme, but differences appeared during ripening. The chicken-pepsin cheeses had poor body and weak Cheddar-cheese flavour, with many and intense off-flavours. The cheeses made with bovine and swine pepsins were only slightly inferior in quality and intensity of Cheddar-cheese flavour to the rennet cheeses. From a simulated cheese-making experiment it was concluded that 30–40 % of the added rennet, bovine pepsin and chicken pepsin was probably inactivated during the cheese-making process and that most or all of the swine pepsin was lost. These results provide an explanation for the variations observed in cheese ripening.It was concluded that chicken pepsin would not prove a suitable rennet substitute for making Cheddar cheese because of the quality of the cheese produced, and that bovine pepsin would not prove suitable because of the cost of preparing a suitable extract. Swine pepsin would appear to be suitable if the ripening time were to be lengthened or if another enzyme were to be added to assist ripening; it is cheaper than rennet and other rennet substitutes.

scholarly journals Lipolytic Activities of Bacteria and Fungi Isolated from Soil Samples

2021 ◽  
pp. 27-43
Author(s):  
Racheal Oluwayemisi Fashogbon ◽  
Bose Adebayo ◽  
Victoria Musa ◽  
Titilayo Femi-Ola
Keyword(s):  
Lipase Activity ◽  
Metal Ion ◽  
Specific Activity ◽  
Soil Samples ◽  
Bacillus Sp ◽  
State University ◽  
Sudan Black B ◽  
Fusarium Sp ◽  
Microbial Lipases ◽  
Bacteria And Fungi

This study was carried out at the Department of Microbiology, Microbiology Laboratory, Ado-Ekiti State University, Ekiti State, Nigeria between July, 2018 to March, 2019. Due to the diverse biotechnological importance of lipases as a biocatalytic enzyme, extracellular production of microbial lipases has to gain lots of interest. This study, therefore, focused on the physicochemical parameters of lipase producing microorganisms from different soil samples. Microorganisms were isolated from four different soil samples using Nutrient Agar (NA) and Potato Dextrose Agar (PDA). The isolates were identified and characterized. Production, an assay for Lipase enzymes, purification, the effect of pH, Temperature and metal ion was investigated. The isolates were culturally, morphologically and biochemically characterized. Two of the bacteria strains (Bacillus sp. and Staphylococcus sp.) and four fungi (Fusarium sp., Aspergillus fumigatus, Aspergillus niger, and Trichophyton sp.) isolates were able to produce lipid using Sudan Black B Fat staining techniques. Fusarium sp. isolated from dumpsite soil had the highest specific lipase activity (21.16 µmol/min/ml) while Bacillus sp. isolated from red oil spill soil had the highest lipase activity (0.59 µmol/min/mg). The specific activity of partially purified lipase for Fusarium sp. was 2.39 µmol/min/mg while Bacillus sp. had a specific activity of 2.46 µmol/min/mg. 30oC - 50oC, pH 7.0 to 9.0 and KCl2 (139.672%) supported the highest production of lipase by the Bacillus sp. and Fusarium sp. This study demonstrated that the Bacillus sp. produced a high amount of lipase activity followed by Fusarium sp. Extensive and persistent screening for new microorganisms and their lipolytic activities will help to provide faster ways to solve most environmental soil pollution.

Modulation of Integrin Function in Hematopoietic Progenitor Cells by CD43 Engagement: Possible Involvement of Protein Tyrosine Kinase and Phospholipase C-γ

Blood ◽  
1999 ◽  
Vol 93 (10) ◽  
pp. 3317-3326 ◽  
Author(s):  
Naoyuki Anzai ◽  
Akihiko Gotoh ◽  
Hirohiko Shibayama ◽  
Hal E. Broxmeyer
Keyword(s):  
Tyrosine Kinase ◽  
Phospholipase C ◽  
Protein Tyrosine Kinase ◽  
Kinase Inhibitor ◽  
Hematopoietic Cells ◽  
Cross Linking ◽  
Human Cord Blood ◽  
Protein Tyrosine ◽  
Extracellular Matrix Components ◽  
Almost All

Attachment of cells to extracellular matrix components is critical for the regulation of hematopoiesis. CD43 is a mucin-like transmembrane sialoglycoprotein expressed on the surface of almost all hematopoietic cells. A highly extended structure of extracellular mucin with negative charge may function as a repulsive barrier to hematopoietic cells. However, some investigators have shown that CD43 has proadhesive properties, and engagement of CD43 has been reported to upregulate integrin-mediated cell adhesion in T cells. We found that cross-linking of CD43 with monoclonal antibodies (MoAbs) enhanced integrin 4β1 (very late antigen [VLA]-4) and 5 β1 (VLA-5)-dependent adhesion of human cord blood CD34+ cells to fibronectin. CD34+ CD38hi, but not CD34+CD38−/low cells responded significantly to the stimulus, suggesting that committed, but not stem and more immature progenitors are sensitive to CD43-mediated activation of integrin. To elucidate the molecular mechanism leading to integrin activation, we used the growth factor-dependent cell line MO7e. Cross-linking of CD43 induced tyrosine phosphorylation of several intracellular molecules including the protein tyrosine kinase Syk, the proto-oncogene product Cbl, and phospholipase C (PLC)-γ2 in MO7e cells. Moreover, protein tyrosine kinase inhibitor herbimycin A and PLC inhibitor U73122 both blocked CD43-induced enhancement of adhesion to fibronectin. These results indicate that signals mediated through CD43 may increase integrin affinity to fibronectin via a pathway dependent on protein tyrosine kinase and PLC-γ activation in hematopoietic progenitors.

Denaturation of porcine pepsin during Cheddar cheese manufacture

1977 ◽  
Vol 44 (2) ◽  
pp. 335-343 ◽  
Author(s):  
A. M. O'Keeffe ◽  
P. F. Fox ◽  
C. Daly
Keyword(s):  
Cheddar Cheese ◽  
Porcine Pepsin ◽  
Cheese Making ◽  
Temperature Range ◽  
Cheese Ripening ◽  
Cheese Curd

SummaryPorcine pepsin was rapidly denatured in phosphate buffers, pH 6·4–6·7, in the temperature range 31–39 °C and was only slightly more stable in milk under similar conditions. However, the enzyme was considerably more stable in Cheddar cheese curd in which the extent of denaturation was very markedly influenced by the pH of the milk at setting. Under normal cheese-making conditions, porcine pepsin was about equally stable with chymosin. Two modifications of the cheesemanufacturing procedure were developed which permit the manufacture of cheese almost free of coagulant and suitable for the assessment of the contribution of starter proteinases to proteolysis during cheese ripening.

Pattern of Eprinomectin Milk Excretion in Dairy Sheep Unaffected by Lactation Stage: Comparative Residual Profiles in Dairy Products

2006 ◽  
Vol 69 (10) ◽  
pp. 2424-2429 ◽  
Author(s):  
FERNANDA IMPERIALE ◽  
ALEJANDRA PIS ◽  
JUAN SALLOVITZ ◽  
ADRIÁN LISFCHITZ ◽  
MARGARITA BUSETTI ◽  
...  
Keyword(s):  
Dairy Products ◽  
High Performance ◽  
Maximum Residue Limit ◽  
Dairy Sheep ◽  
Cheese Making ◽  
Cheese Ripening ◽  
Lactation Stage ◽  
Low Concentrations ◽  
The Relationship ◽  
Kinetics Of

Eprinomectin (EPM) is a broad-spectrum endectocide compound approved for use in dairy cattle with a zero milk-withdrawal period, but has not been registered for use in lactating dairy sheep. The pattern of EPM excretion in milk was comparatively characterized following its pour-on administration (500 μg/kg) to lactating dairy sheep at two different stages of lactation. The relationship between milk excretion and plasma disposition kinetics of EPM was characterized. Residual EPM concentrations were assessed during cheese making (whey and curd) and ripening (cheese) by high-performance liquid chromatography and fluorescence detection. EPM was poorly distributed from the bloodstream to the mammary gland and low concentrations were excreted in milk. The level of milk production (early-mid and mid-late lactation) did not affect either the plasma-milk distribution or the pattern of residual concentrations in milk. During cheese making, the highest residual concentrations of EPM were measured in the curd, which increased during cheese ripening, reaching a maximum after 40 days. However, these residual concentrations were below the maximum residue limit of 20 ng/ml established for EPM in bovine's milk. Therefore, these dairy products could be considered safe for consumers after the EPM antiparasitic pour-on treatment (500 μg/kg) in lactating dairy sheep.

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