Dynamic changes in the physiochemical, structural, and flavor characteristics of ginger-juice milk curd were explored by texture analysis, scanning electron microscopy, rheometry, electronic tongue, and gas chromatography-mass spectrometry (GC-MS). Protein electrophoresis showed that ginger juice could hydrolyze α_s-, β-, and κ-casein. Curd formation was initiated at 90 s, marked by significant changes in intensity detected via intrinsic fluorescence. The contents of soluble protein and calcium decreased rapidly during coagulation, while the caseinolytic activity, storage moduli, loss moduli, hardness, adhesiveness, and water-holding capacity increased, resulting in a denser gel structure with smaller pores and fewer cavitations as observed by scanning electron microscopy. Electronic tongue analysis indicated that milk could neutralize the astringency and saltiness of ginger juice, rendering the taste of ginger-juice milk curd more akin to that of milk. Approximately 70 volatile components were detected in ginger-juice milk curd. α‍-Zingiberene, α‍-curcumene, β‍-sesquiphellandrene, and β‍-bisabolene were the predominant volatile flavor compounds, exhibiting an initial decrease in content followed by stability after 90 s. Decanoic acid, γ-elemene, and caryophyllene were identified as unique volatile compounds after mixing of milk and ginger juice. Understanding the dynamic changes in these characteristics during coagulation holds significant importance for the production of ginger-juice milk curd.
Zingiber officinale/chemistry* ; Milk/chemistry* ; Animals ; Taste ; Gas Chromatography-Mass Spectrometry ; Caseins/chemistry* ; Microscopy, Electron, Scanning ; Rheology ; Flavoring Agents

BACKGROUNDEnamel decalcification in orthodontics is a concern for dentists and methods to remineralize these lesions are the focus of intense research. The aim of this study was to evaluate the remineralizing effect of casein phosphopeptide amorphous calcium phosphate (CPP-ACP) nanocomplexes on enamel decalcification in orthodontics.

METHODSTwenty orthodontic patients with decalcified enamel lesions during fixed orthodontic therapy were recruited to this study as test group and twenty orthodontic patients with the similar condition as control group. GC Tooth Mousse, the main component of which is CPP-ACP, was used by each patient of test group every night after tooth-brushing for six months. For control group, each patient was asked to brush teeth with toothpaste containing 1100 parts per million (ppm) of fluoride twice a day. Standardized intraoral images were taken for all patients and the extent of enamel decalcification was evaluated before and after treatment over this study period. Measurements were statistically compared by t test.

RESULTSAfter using CPP-ACP for six months, the enamel decalcification index (EDI) of all patients had decreased; the mean EDI before using CPP-ACP was 0.191 ± 0.025 and that after using CPP-ACP was 0.183 ± 0.023, the difference was significant (t = 5.169, P < 0.01). For control group, the mean EDI before treatment was 0.188 ± 0.037 and that after treatment was 0.187 ± 0.046, the difference was not significant (t = 1.711, P > 0.05).

CONCLUSIONCPP-ACP can effectively improve the demineralized enamel lesions during orthodontic treatment, so it has some remineralization potential for enamel decalcification in orthodontics.

Adolescent ; Caseins ; chemistry ; therapeutic use ; Dental Enamel ; drug effects ; Female ; Humans ; Male ; Orthodontics ; methods

This study focused on the contamination mechanism and regeneration strategies of sulfopropyl ion exchange resin (SP Sepharose FF) during the separation of recombinant human lactoferrin from transgenic bovine milk. We analyzed primary constituents' contents in chromatorgraphic material and fractions. The results showed that the lipid in milk can clog the column or adhere to the resin through hydrophobic interaction, leading to an increase in column pressure. Some casein molecules were found to adsorb onto the resin through electrostatic interaction, therefore the adsorption capacity was decreased. There was no direct interaction between lactose and the resin in the chromatorgraphic process. Increased continuous chromatographic cycles and prolonged time interval between protein purification and column regeneration could enhance the undesirable interaction between the contaminants and resin, thus lowering the regeneration efficiency. NaOH was found to be effective in the removal of lipid and casein molecules from the column. Furthermore, normal microstructure and chromatographic performance of the ion exchanger was recovered after this cleaning procedure.
Adsorption ; Animals ; Animals, Genetically Modified ; genetics ; metabolism ; Caseins ; chemistry ; Cattle ; Chromatography, Ion Exchange ; methods ; Female ; Humans ; Ion Exchange Resins ; chemistry ; Lactoferrin ; biosynthesis ; genetics ; isolation & purification ; Mammary Glands, Animal ; metabolism ; Milk ; chemistry ; Milk Proteins ; isolation & purification ; metabolism ; Recombinant Proteins ; biosynthesis ; genetics ; isolation & purification ; Sodium Hydroxide ; chemistry

Because of the complexity of the cathepsin B-like (CBL) family, an information on the biological and biochemical characteristics of individual CBL genes is lacking. In this study, we investigated the degradative effects of the recombinant HC58 protein isolated from Haemonchus contortus parasites on protein substrates over a broad pH range in vitro. This protein, which hydrolyzed the synthetic peptide substrates Z-FR-AMC and Z-RR-AMC, had characteristics of the cysteine protease class of proteins. In the acidic pH range, the isolated protein actively degraded hemoglobin (Hb), the heavy chain of goat immunoglobulin G, and azocasein. By contrast, it degraded fibrinogen in the alkaline pH range. These activities were strongly inhibited in the presence of the cysteine protease inhibitor E-64. While the protein digested Hb, it did not induce the agglutination of erythrocytes from its natural host. These results suggest that the HC58 protein may play a role in the nutrition of this parasite.
Animals ; Caseins/metabolism ; Cathepsin B/antagonists&inhibitors/*genetics/isolation & purification/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; DNA, Complementary/genetics ; Goat Diseases/*parasitology ; Goats ; Haemonchiasis/parasitology/*veterinary ; Haemonchus/*enzymology/genetics/isolation & purification ; Hemagglutination Tests/veterinary ; Hemoglobins/metabolism ; Hydrogen-Ion Concentration ; Immunoglobulin G/metabolism ; Leucine/analogs & derivatives/pharmacology ; RNA, Helminth/chemistry/genetics ; Recombinant Proteins/genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction/veterinary

Whey protein concentrate (WPC 80) and sodium caseinate were hydrolyzed by Protamex to 5%, 10%, 15%, and 20% degree of hydrolysis (DH). WPC 80, sodium caseinate and their hydrolysates were then analyzed, compared and evaluated for their nutritional qualities. Their chemical composition, protein solubility, amino acid composition, essential amino acid index (EAA index), biological value (BV), nutritional index (NI), chemical score, enzymic protein efficiency ratio (E-PER) and in vitro protein digestibility (IVPD) were determined. The results indicated that the enzymatic hydrolysis of WPC 80 and sodium caseinate by Protamex improved the solubility and IVPD of their hydrolysates. WPC 80, sodium caseinate and their hydrolysates were high-quality proteins and had a surplus of essential amino acids compared with the FAO/WHO/UNU (1985) reference standard. The nutritive value of WPC 80 and its hydrolysates was superior to that of sodium caseinate and its hydrolysates as indicated by some nutritional parameters such as the amino acid composition, chemical score, EAA index and predicted BV. However, the E-PER was lower for the WPC hydrolysates as compared to unhydrolyzed WPC 80 but sodium caseinate and its hydrolysates did not differ significantly. The nutritional qualities of WPC 80, sodium caseinate and their hydrolysates were good and make them appropriate for food formulations or as nutritional supplements.
Amino Acids ; chemistry ; Caseins ; chemistry ; metabolism ; Dietary Proteins ; analysis ; Evaluation Studies as Topic ; Hydrolysis ; Milk Proteins ; chemistry ; metabolism ; Models, Statistical ; Nutritive Value ; Protein Hydrolysates ; chemistry ; Solubility ; Temperature ; Time Factors ; Tryptophan ; chemistry ; Whey Proteins