scholarly journals Phenylarsine Oxide Can Induce the Arsenite-Resistance Mutant PML Protein Solubility Changes

2017 ◽  
Vol 18 (2) ◽  
pp. 247 ◽  
Author(s):  
Yu Jiang ◽  
Ye Chen ◽  
Chao Wang ◽  
Yong Lan ◽  
Chang Yang ◽  
...  
2019 ◽  
Vol 15 (3) ◽  
pp. 228-233
Author(s):  
Prabhavathi Supriya ◽  
Kandikere R. Sridhar

Background: Utilization of wild legumes has received prime importance in the recent past to compensate the scarcity of protein-rich foods as well as to tackle the protein energy malnutrition. Ripened split beans of Canavalia maritima devoid of seed coat and testa serve as traditional nutraceutical source for the coastal dwellers of Southwest India. Objective: The present study projects proximal and functional attributes of uncooked and cooked ripened split beans of C. maritima to be used in the preparation of functional foods. Methods: Proximal properties (moisture, crude protein, total lipids, crude fibre, carbohydrates and calorific value) and functional properties (protein solubility, gelation capacity, water-absorption, oilabsorption, emulsion qualities and foam qualities) of split beans were evaluated by standard methods. Results: Cooking did not significantly changed the crude protein, total lipids, ash, carbohydrates and calorific value, while it significantly increased the crude fibre. The protein solubility, water-absorption capacity, foam capacity and foam stability were significantly higher in uncooked than cooked beans. The cooked beans were superior to uncooked beans in least gelation concentration, low oil-absorption capacity, emulsion activity and emulsion stability. Conclusion: The functional properties of split bean flours were influenced by the proximal components like crude protein, total lipids and crude fibre. The energy-rich ripened split beans of C. maritima can serve as a new potential source for production of value added functional foods owing to their rich protein, rich carbohydrates, low-lipid and potential bioactive attributes.


Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 969
Author(s):  
Xingyi Jiang ◽  
Qinchun Rao

Fish allergy is a life-long food allergy whose prevalence is affected by many demographic factors. Currently, there is no cure for fish allergy, which can only be managed by strict avoidance of fish in the diet. According to the WHO/IUIS Allergen Nomenclature Sub-Committee, 12 fish proteins are recognized as allergens. Different processing (thermal and non-thermal) techniques are applied to fish and fishery products to reduce microorganisms, extend shelf life, and alter organoleptic/nutritional properties. In this concise review, the development of a consistent terminology for studying food protein immunogenicity, antigenicity, and allergenicity is proposed. It also summarizes that food processing may lead to a decrease, no change, or even increase in fish antigenicity and allergenicity due to the change of protein solubility, protein denaturation, and the modification of linear or conformational epitopes. Recent studies investigated the effect of processing on fish antigenicity/allergenicity and were mainly conducted on commonly consumed fish species and major fish allergens using in vitro methods. Future research areas such as novel fish species/allergens and ex vivo/in vivo evaluation methods would convey a comprehensive view of the relationship between processing and fish allergy.


2021 ◽  
Vol 6 (1) ◽  
Author(s):  
Hai-Lin Dong ◽  
Jia-Qi Li ◽  
Gong-Lu Liu ◽  
Hao Yu ◽  
Zhi-Ying Wu

AbstractSorbitol dehydrogenase gene (SORD) has been identified as a novel causative gene of recessive forms of hereditary neuropathy, including Charcot–Marie–Tooth disease type 2 and distal hereditary motor neuropathy (dHMN). Our findings reveal two novel variants (c.404 A > G and c.908 + 1 G > C) and one known variant (c.757delG) within SORD in four Chinese dHMN families. Ex vivo cDNA polymerase chain reaction confirmed that c.908 + 1 G > C variant was associated with impaired splicing of the SORD transcript. In vitro cell functional studies showed that c.404 A > G variant resulted in aggregate formation of SORD and low protein solubility, confirming the pathogenicity of SORD variants. We have provided more evidence to establish SORD as a causative gene for dHMN.


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