The Effect of Liposome Encapsulation of Chymosin Derived by Fermentation on Manchego Cheese Ripening

Picón, Antonia; Gaya, Pilar; Médina, Margarita; Núñez, Manuel

doi:10.3168/jds.s0022-0302(94)76923-x

Cited by 55 publications

(30 citation statements)

References 17 publications

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“…As is shown in Figure 4B, HCA distributed the samples in three main groups, including control samples (C), starter free cheeses (S) and rennet free cheeses (R). As PC1 explained most the variation between the control and experimental cheeses, suggesting that the peptides which contributed to the variation between these samples mostly eluted in the chromatogram at retention times shorter than 35 min and thus could be considered hydrophilic [14,30,38]. …”

Section: Rp-hplcmentioning

confidence: 99%

Contribution of rennet and starter to proteolysis in Iranian UF white cheese

Hesari

Ehsani

Khosroshahi

et al. 2006

Lait

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-The relative contributions of rennet and starter to proteolysis during the storage of ultrafiltered (UF) Iranian white cheese were investigated. In the experimental design used, starter and rennet were, in separate treatments, omitted and gluconic acid-δ-lactone was used for acidification of starter-free samples. The experimental treatments used did not have significant effects on composition. Omission of rennet in manufacture significantly reduced proteolysis during ripening of UF white cheese, and caused differences in peptide profiles determined by both urea-polyacrylamide gel electrophoresis and reversed-phase HPLC; omission of starter had a considerably smaller effect on these parameters. In cheeses made without rennet, noticeable casein degradation was not observed suggesting little contribution of indigenous proteinases to proteolysis during the ripening of UF Iranian white cheese. Both rennet and starter contributed indirectly or directly to production of free amino acids in UF white cheese and omission of either of these agents strongly reduced production of FAA during ripening. Résumé -Contribution de la présure et des ferments à la protéolyse du fromage iranien de type pâte fraîche fabriqué par ultrafiltration (UF). Les contributions relatives de la présure et des ferments à la protéolyse du fromage iranien de type pâte fraîche fabriqué par ultrafiltration ont été étudiées au cours du stockage. L'expérimentation comportait respectivement un essai sans pré-sure et un essai sans ferment. L'acidification des fabrications sans ferment a été réalisée à l'aide de glucono-delta-lactone. Les différents traitements n'avaient pas d'effet significatif sur la composition. L'omission de la présure au cours de la fabrication réduisait de façon significative la protéolyse au cours de la maturation du fromage à pâte fraîche fabriqué par UF, et provoquait des différences dans les profils peptidiques observés aussi bien par électrophorèse sur gel polyacrylamide-urée que par chromatographie liquide en phase inverse ; l'omission de ferment avait un effet considérable-ment moins marqué sur ces paramètres. Dans les fromages fabriqués sans présure, aucune dégrada-tion perceptible de la caséine n'a été observée, suggérant ainsi une faible contribution des protéases endogènes à la protéolyse au cours de la maturation du fromage iranien de type pâte fraîche fabriqué par UF. La présure et les ferments contribuaient tous deux indirectement ou directement à la production des acides aminés libres dans le fromage UF à pâte fraîche et l'omission de l'un ou de l'autre de ces agents réduisait fortement la production des acides aminés libres au cours de la maturation. fromage à pâte fraîche iranien / ultrafiltration / présure / ferment / protéolyse Iranian white cheese / ultrafiltration / rennet / starter / proteolysis

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Section: Rp-hplcmentioning

confidence: 99%

Contribution of rennet and starter to proteolysis in Iranian UF white cheese

Hesari

Ehsani

Khosroshahi

et al. 2006

Lait

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“…Recently, liposome, spherical particles with sizes at the range of the nanometer to micrometer formed by polar lipids (Charcosset 2009;Taylor et al 2005) has received special attention in the literature (Mozafari et al 2008a, b). Liposome technology has generated much interest in food industry for the encapsulation of different materials such as ferrous glycinate (Ding et al 2011), ferrous sulfate (Xia and Xu 2005), antioxidant (Mozafari et al 2006), nisin (Taylor et al 2007;Laridi et al 2003;Colas et al 2007) β-galactosidase (Rao et al 1994) and different cheese accelerated enzymes such as lipase (Kheadr et al 2002), Nutrease (Alkhalaf et al 1989), chymotripsine (Laloy et al 1998;Dufour et al 1996), chymosine (Picon et al 1994), neutral protease (Picon et al 1995), cyprosine (Picon et al 1996) bacterial and fungal protease, Flavourzyme and palatase . Different methods such as reverse-phase evaporation, dehydration-rehydration, microfludization technique and proliposome usage have been applied for liposome manufacturing with a variation of EE (%) ranging from 10 to 40.3 %.…”

Section: Introductionmentioning

confidence: 99%

The encapsulation of flavourzyme in nanoliposome by heating method

et al. 2013

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The main objective of this study was to use heating method (HM) to prepare liposome without employing any chemical solvent or detergent. Plackett-Burman design (PBD) was applied for the screening of significant process variables including the lecithin proportion, the cholesterol/ lecithin ratio, the pH of solution for liposome preparation, the enzyme/lecithin ratio, the stirring time, the process temperature, the speed of stirrer, the ratio of stirrer to the tank diameter, the application of homogenization, the method of adding enzyme and centrifugation conditions on the encapsulation efficiency (EE %) of liposome and the activity of liposomal Flavourzyme (LAPU −1 ) (P<0.05). Then, the response surface methodology based on the central composite design (CCD) was applied for the evaluation of the impacts of the significant mentioned variables on the EE (%) and the activity of the liposomal Flavourzyme. The results indicated that the lecithin proportion and the stirring time were the major influential variables for both responses. The most suitable formulation of the Flavourzyme-loaded liposome is 4.5 % lecithin, 45°C temperature, 5 % Flavourzyme/lecithin ratio, 30 min stirring time and medium pH of 6. Under suitable operating conditions, the EE of liposome and the activity of the liposomal Flavourzyme were achieved as 26.5 % and 9.96 LAPU ml −1 , respectively. AFM technique and size distribution clearly showed the diameter of 189 nm for the spherical shape of the Flavourzyme-loaded nanoliposome.

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“…However, cheese texture could be affected by the introduction of lipid vesicles [18,24]. Another drawback is that most of the methods used for liposome preparation require organic sol vents and are difficult to use on a large-scale in the food industry [27].…”

Section: Introductionmentioning

confidence: 99%

“…The addition of extra amounts of ripening enzymes is a solution of preference [7]. Among the different methods of enzyme addition proposed, the encapsulation of enzymes in liposomes has recently become the subject of renewed interest [8, 24,26,28].…”

Section: Introductionmentioning

confidence: 99%