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1.
J Adv Nurs ; 79(3): 865-884, 2023 Mar.
Article in English | MEDLINE | ID: mdl-35511714

ABSTRACT

AIMS: To investigate and describe the current state of knowledge about Fundamental Care in terms of population, contexts, concepts and gaps. DESIGN: A scoping review. DATA SOURCES: CINAHL, Medline, PsycINFO and EMBASE databases were searched in April 2021 for eligible literature, published from January 2010, onwards. REVIEW METHODS: This scoping review was built around the recommendations of Peters et al. (2020 version). Two researchers conducted the literature search, and three researchers independently screened the titles and abstracts of the retrieved studies' data, using the eligibility criteria and the review questions as a guide. RESULTS: The search yielded 763 records, of which 107 were included. Results are presented under seven subheadings: (a) Countries and Continents, (b) Context, (c) Research Design, (d) Publishing/Journal, (e) Participants and Population, (f) Keywords and (g) Fundamental of Care Framework and Practice Process. All the retrieved articles describe the current state of knowledge about Fundamental Care in terms of population, contexts, concepts and gaps. CONCLUSION: This scoping review highlighted the elevated number of articles that have been published since the beginning of the work on Fundamental Care, 10 years ago. The included articles are related to different dimensions of research, practice and teaching and to the Fundamentals of Nursing Care, but also to nursing theory. Finally, most of the articles had a nursing focus. IMPACT: The results of this scoping review allow us to highlight the work from the past 10 years. This may be of interest to learn more about the research surrounding Fundamental Care. This scoping review allows us to better target the theoretical and empirical developments to focus on in the coming years.


Subject(s)
Nursing Care , Humans , Learning , Nursing Theory
2.
3 Biotech ; 12(10): 253, 2022 Oct.
Article in English | MEDLINE | ID: mdl-36060894

ABSTRACT

Xerophilic Aspergillus molds isolated from halo-alkaliphilic and dry environments are attractive genetic resources for obtaining salt- and osmo-adaptive enzymes. A. sydowii MA0196 secreted the largest amount of γ-glutamyl transpeptidase (GGT) during solid-state fermentation at a low initial water activity (a w = 0.85). Gel filtration analysis revealed that the molecular mass of the purified native enzyme (MA0196 GGT) was 120 kDa. SDS-PAGE analysis showed that MA0196 GGT consists of two subunits with molecular masses of 56.4 and 33 kDa, indicating production from a proenzyme via autoproteolysis. Deglycosylation of the subunits by N-glycosidase F yielded 40.9 and 19.6 kDa species. MA0196 GGT retained transpeptidase and hydrolysis activities and their catalytic efficiency (k cat/K m) under high salt and low water activity. The enzyme displayed broad substrate specificity toward γ-glutamyl acceptors such as amino acids and the imidazole dipeptides, carnosine and anserine. Carnosine and L-glutamine were converted into γ-glutamyl-ß-alanyl-L-histidine by MA0196 GGT with a 32.9% yield in the presence of 2% (v/v) dimethyl sulfoxide. Phylogenetic analysis indicated that MA0196 GGT forms a distinct lineage from A. oryzae and A. sojae GGTs. These excellent properties indicate that MA0196 GGT can be used in salted fermentation and for producing bioactive peptides. Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-022-03259-3.

3.
Int J Food Microbiol ; 353: 109299, 2021 Sep 02.
Article in English | MEDLINE | ID: mdl-34153828

ABSTRACT

A mild-flavored soup stock made from katsuobushi is an important element of traditional Japanese cuisine and is the basic seasoning responsible for the taste. Fermented and ripened katsuobushi, known as karebushi, is manufactured by simmering skipjack tuna that is then smoke-dried, fermented, and ripened in a repeated molding process by five dominant Aspergillus species. Here, our aim was to characterize and identify the lipolytic enzymes secreted by the dominant Aspergillus species, especially A. chevalieri and A. pseudoglaucus, which are involved in hydrolyzing lipids during the molding process. The crude enzyme preparations from the five Aspergillus spp. cultivated on katsuobushi solid medium hydrolyzed triglycerides in fish oil, and more saturated and unsaturated fatty acids (C16:0, C16:1, C18:0, C18:1) were produced than major polyunsaturated fatty acids (C20:5, C22:6). On the basis of ion exchange chromatograms, the composition of the lipolytic enzymes was different in the five species. There was at least one active fraction with high hydrolytic activity toward fish oil in four of the Aspergillus spp., but not A. sydowii; the lipolytic enzyme secreted by A. sydowii had quite high activity toward the artificial substrate p-nitrophenyl butyrate, but low activity toward the natural oil. The lipolytic fractions from A. chevalieri and A. pseudoglaucus were further purified by hydrophobic interaction chromatography then gel-filtration chromatography; LC-MS-MS Mascot analysis identified a variety of lipolytic enzymes, including cutinase, esterase, phospholipase, and carboxyl esterase in the lipolytic fractions from these species. The identified enzymes had 30%-70% identity to previously reported or manually annotated lipases or esterases from taxa other than Aspergillus. The different lipolytic enzymes likely acted on triglycerides in the katsuobushi fish oil. Furthermore, catalase B and Cu/Zn superoxide dismutase, which limit oxidative damage of lipids, were also identified. These antioxidant enzymes may prevent lipid oxidation and rancidity as the lipolytic enzymes hydrolyze lipids during the long fermentation and ripening process. Umami and richness tastes tended to increase in extracts from culture of protease- and peptidase-producing A. sydowii. Our results will aid in the selection and application of desirable strains of Aspergillus species as starter cultures to improve the storage and quality of fermented and ripened karebushi.


Subject(s)
Antioxidants , Fermentation , Food Microbiology , Lipid Metabolism , Lipolysis , Tuna , Animals , Aspergillus/enzymology , Tuna/metabolism , Tuna/microbiology
4.
Int J Food Microbiol ; 327: 108654, 2020 Aug 16.
Article in English | MEDLINE | ID: mdl-32416377

ABSTRACT

A soup stock made from katsuobushi is an important element of, and the basic seasoning responsible for the taste of, traditional Japanese cuisine. Fermented and ripened katsuobushi, called karebushi, is manufactured via a repeated molding process on the katsuobushi surface. Our aim was to characterize the surface Aspergillus community and their enzymes involved in the fermentation and ripening. Five dominant Aspergillus species isolated from the karebushi surface were identified-A. amstelodami, A. chevalieri, A. pseudoglaucus, A. ruber, and A. sydowii. Analyses were performed on final molding stage-samples from different manufacturers, and 1st to 4th molding stage-samples from the same manufacturer. The composition ratios of the five Aspergillus spp. varied according to the manufacturer of the karebushi. A. amstelodami and A. chevalieri tended to be detected as dominant species when the water content of the karebushi fillet was >15% and the fat content was >3.5%, respectively. In samples from a given manufacturer, the dominant species in the final molding stage tended to be A. chevalieri and A. pseudoglaucus. Mixed molds were cultured by solid-state fermentation using katsuobushi powder medium at two different water activity (aw) levels. Crude extracts from each culture showed lipase, aminopeptidase, carboxypeptidase, and protease activities. Notably, the crude extracts cultivated at 0.85 aw showed higher protease activity toward hemoglobin and lipase activity toward p-nitrophenyl palmitate than those at 0.95 aw. These hydrolytic enzymes are probably involved in decolorization of katsuobushi and lipid degradation during the long fermentative and ripening period. In addition, mixed cultures could transform 2,6-dimethoxyphenol into 1,2,3-trimethoxybenzene, previously reported as an attractive and mild flavor component. Our results may help promote the use of desirable Aspergillus spp. as starter cultures for manufacturers to stabilize and improve the quality of fermented and ripened karebushi.


Subject(s)
Aspergillus/physiology , Fermentation , Fermented Foods/microbiology , Fish Products/microbiology , Food Microbiology , Animals , Fish Products/standards , Hydrolysis , Lipase/metabolism
5.
J Sci Food Agric ; 99(4): 2042-2047, 2019 Mar 15.
Article in English | MEDLINE | ID: mdl-30187473

ABSTRACT

BACKGROUND: The xerophilic Aspergillus molds, Aspergillus glaucus and Aspergillus repens, have been used in the ripening and fermentation of dried tuna bonito (katsuobushi). These molds, and especially their extracellular hydrolytic enzymes, may also be of wider industrial value. RESULTS: Aspergillus glaucus strain MA0196 produces different types of hydrolytic enzymes, including amylase, serine protease, aspartic protease, lipase and cellulase, depending on the composition of the medium. We characterized several of these enzymes, focusing on a glycosylated aspartic protease. The results showed that the lower the d-glucose concentration in the medium, the higher the degree of protease glycosylation, with excess glycosylation tending to decrease protease activity. The molecular mass of the glycosylated protease as determined by gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis was 243 and 253 kDa, respectively. The chemically deglycosylated protease had a molecular mass of only 46 kDa. The amount of myoglobin-decolorizing activity was similar to that of a previously reported aspartic protease from A. repens strain MK82. However, the strain MA0196 protease more broadly hydrolyzed myoglobin and hemoglobins than did the strain MK82 protease. CONCLUSION: The results of the present study demonstrate the potential utility of Aspergillus molds as a functionally new microbial resource for industrial applications such as the bleaching of heme proteins. © 2018 Society of Chemical Industry.


Subject(s)
Aspartic Acid Proteases/chemistry , Aspergillus/enzymology , Fungal Proteins/chemistry , Hemoglobins/chemistry , Myoglobin/chemistry , Aspartic Acid Proteases/isolation & purification , Aspartic Acid Proteases/metabolism , Aspergillus/chemistry , Aspergillus/genetics , Biocatalysis , Fungal Proteins/isolation & purification , Fungal Proteins/metabolism , Heme/chemistry , Hydrogen-Ion Concentration , Hydrolysis , Molecular Weight
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