Protein Solubility and Aggregation in Bacteria

2016 ◽  
Keyword(s):  
Protein Solubility

Proximal and Functional Properties of Edible Ripened Split Beans of Coastal Wild Legume Canavalia maritima

2019 ◽  
Vol 15 (3) ◽  
pp. 228-233
Author(s):  
Prabhavathi Supriya ◽  
Kandikere R. Sridhar
Keyword(s):  
Water Absorption ◽  
Functional Properties ◽  
Crude Protein ◽  
Functional Foods ◽  
Protein Solubility ◽  
Calorific Value ◽  
Absorption Capacity ◽  
Total Lipids ◽  
Crude Fibre ◽  
Protein Rich

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.

scholarly journals Effect of Processing on Fish Protein Antigenicity and Allergenicity

Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 969
Author(s):  
Xingyi Jiang ◽  
Qinchun Rao
Keyword(s):  
Fish Species ◽  
Protein Denaturation ◽  
Ex Vivo ◽  
Protein Solubility ◽  
Future Research ◽  
Food Protein ◽  
In Vivo Evaluation ◽  
Fish Allergy

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.

scholarly journals Biallelic SORD pathogenic variants cause Chinese patients with distal hereditary motor neuropathy

2021 ◽  
Vol 6 (1) ◽  
Author(s):  
Hai-Lin Dong ◽  
Jia-Qi Li ◽  
Gong-Lu Liu ◽  
Hao Yu ◽  
Zhi-Ying Wu
Keyword(s):  
Ex Vivo ◽  
Protein Solubility ◽  
Chinese Patients ◽  
Hereditary Neuropathy ◽  
Motor Neuropathy ◽  
Causative Gene ◽  
Hereditary Motor ◽  
Functional Studies ◽  
Hereditary Motor Neuropathy

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.

Effects of ultrasound extraction on the physicochemical and emulsifying properties of rice bran protein

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Li-Hui Sun ◽  
Feng Yu ◽  
Yu-Ying Wang ◽  
Shi-Wen Lv ◽  
Lei-Yu He
Keyword(s):  
Rice Bran ◽  
Protein Solubility ◽  
Surface Hydrophobicity ◽  
Absorption Capacity ◽  
Emulsifying Properties ◽  
Ultrasound Assisted Extraction ◽  
Suitable Alternative ◽  
Rice Bran Protein ◽  
Assisted Extraction ◽  
Ultrasound Assisted

Abstract In this study, rice bran protein was prepared by ultrasound-assisted extraction, and its physicochemical and emulsifying properties were also evaluated. Results demonstrated that a significant increase in protein yield was observed when ultrasound-assisted method was employed for extracting protein. Noticeably, obtained rice bran protein possessed excellent physicochemical properties, such as oil absorption capacity, protein solubility and foaming property. More hydrophobic groups were exposed in the process of ultrasound-assisted extraction, which led to the increase of surface hydrophobicity. More importantly, the ultrasound-assisted extraction could improve emulsifying properties of rice bran protein, and the emulsions prepared using protein samples exhibited the great stability. Besides, it was also found that emulsifying properties of protein samples presented a decrease trend with increasing ultrasound power and time. All in all, ultrasound-assisted extraction is a suitable alternative process for preparing rice bran protein.

Functional Properties of the Protein Isolate and Major Fractions of Pine Nut Proteins Prepared from the Changbai Mountain in China

2014 ◽  
Vol 881-883 ◽  
pp. 766-775 ◽  
Author(s):  
Dan Wu ◽  
Wei Hong Min ◽  
Jing Sheng Liu ◽  
Li Fang ◽  
Hong Mei Li ◽  
...  
Keyword(s):  
Amino Acids ◽  
Functional Properties ◽  
Protein Solubility ◽  
Essential Amino Acids ◽  
Protein Isolate ◽  
Absorption Capacity ◽  
Changbai Mountain ◽  
Major Protein ◽  
Pine Nut ◽  
A Value

The functional properties of protein isolate and major protein fractions prepared from Changbai Mountain pine nuts were investigated. Albumin, globulin, glutelin, and protein isolates were obtained after the Osborne method and alkaline dissolution and acid precipitation, and protein contents of the fractions are 48.02%, 81.93%, 83.02%, and 89.69%, respectively. For the sulfhydryl contents, albumin is the highest, and glutelin is the lowest. In a disulphide bond, the protein isolate content is the highest with a value of 28.74 μmol/g, and the glutelin content is the lowest with the value of 13.46 μmol/g. For the four kinds of proteins, the essential amino acids in percentage of total amino acids are 31.13%, 34.22%, 30.30%, and 34.54%, respectively. The pH dependent protein solubility profile reveals that the minimum solubility is at pH 5.0, which corresponds to the isoelectric point. Protein isolate has the minimum water absorption capacity with a value of 0.59 ml/g. On the other hand, albumin has the minimum oil absorption capacity with a value of 2.11 ml/g. The emulsifying activity and stability and the foaming activity and stability increased with increasing concentration of four kinds of proteins. SDS-PAGE results showed that these four kinds of proteins have different molecules.

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