Structural and Functional Characterization of Two Pennisetum sp. Biomass during Ultrasono-Assisted Alkali Pretreatment and Enzymatic Hydrolysis for Understanding the Mechanism of Targeted Delignification and Enhanced Saccharification

2017 ◽  
Vol 5 (8) ◽  
pp. 6486-6497 ◽  
Author(s):  
Sonali Mohapatra ◽  
Sivakumar Pattathil ◽  
Hrudayanath Thatoi
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Characterization ◽  
Alkali Pretreatment

scholarly journals Hydrolysis Process Optimization and Functional Characterization of Yak Skin Gelatin Hydrolysates

2019 ◽  
Vol 2019 ◽  
pp. 1-11
Author(s):  
Hui Yang ◽  
Yanting Xue ◽  
Jiaheng Liu ◽  
Shunyi Song ◽  
Lei Zhang ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Characterization ◽  
Meat Production ◽  
Degree Of Hydrolysis ◽  
Foaming Properties ◽  
The Tibetan Plateau ◽  
Hydrolysis Process ◽  
Potential Applications ◽  
Central Composite

Yak (Bos grunniens) is an animal mainly living on the Tibetan Plateau. Yak skin is a valuable resource that is wasted in the meat production process. This study aimed to prepare yak skin gelatin hydrolysates (YSGH) from yak skin through enzymatic hydrolysis and investigate functional characterization of YSGH. We showed that trypsin was more effective than neutrase, papain, and pepsin in increasing the degree of hydrolysis (DH) of YSGH. The conditions of enzymatic hydrolysis were optimized using central composite design (CCD) and response surface method (RSM), and the highest DH value of 31.96% was obtained. We then analyzed the amino acid compositions and molecular weight distribution of peptides in YSGH. The obtained YSGH exhibited certain antioxidant activity and excellent ACE-inhibitory activity (IC50 = 0.991 mg/mL). In addition, the solubility (98.79%), emulsification, and foaming properties of YSGH developed here were also evaluated. With these physicochemical and biological functions, YSGH had potential applications in food, pharmaceuticals, and cosmetics as an ingredient.

Functional characterization of human brown adipose tissue metabolism

2020 ◽  
Vol 477 (7) ◽  
pp. 1261-1286 ◽  
Author(s):  
Marie Anne Richard ◽  
Hannah Pallubinsky ◽  
Denis P. Blondin
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Functional Characterization ◽  
Human Infants ◽  
Positron Emission ◽  
Brown Adipose ◽  
Treatment Of Obesity ◽  
And Function

Brown adipose tissue (BAT) has long been described according to its histological features as a multilocular, lipid-containing tissue, light brown in color, that is also responsive to the cold and found especially in hibernating mammals and human infants. Its presence in both hibernators and human infants, combined with its function as a heat-generating organ, raised many questions about its role in humans. Early characterizations of the tissue in humans focused on its progressive atrophy with age and its apparent importance for cold-exposed workers. However, the use of positron emission tomography (PET) with the glucose tracer [18F]fluorodeoxyglucose ([18F]FDG) made it possible to begin characterizing the possible function of BAT in adult humans, and whether it could play a role in the prevention or treatment of obesity and type 2 diabetes (T2D). This review focuses on the in vivo functional characterization of human BAT, the methodological approaches applied to examine these features and addresses critical gaps that remain in moving the field forward. Specifically, we describe the anatomical and biomolecular features of human BAT, the modalities and applications of non-invasive tools such as PET and magnetic resonance imaging coupled with spectroscopy (MRI/MRS) to study BAT morphology and function in vivo, and finally describe the functional characteristics of human BAT that have only been possible through the development and application of such tools.

Functional Characterization of PM6/13, a β3-specific (GPIIIa/CD61) Monoclonal Antibody that Shows Preferential Inhibition of Fibrinogen Binding over Fibronectin Binding to Activated Human Platelets

1998 ◽  
Vol 79 (01) ◽  
pp. 177-185 ◽  
Author(s):  
Ashia Siddiqua ◽  
Michael Wilkinson ◽  
Vijay Kakkar ◽  
Yatin Patel ◽  
Salman Rahman ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Platelet Aggregation ◽  
Platelet Rich Plasma ◽  
Functional Characterization ◽  
Human Platelets ◽  
Western Blots ◽  
Activated Platelets ◽  
Reducing Conditions ◽  
Fibronectin Binding

SummaryWe report the characterization of a monoclonal antibody (MAb) PM6/13 which recognises glycoprotein IIIa (GPIIIa) on platelet membranes and in functional studies inhibits platelet aggregation induced by all agonists examined. In platelet-rich plasma, inhibition of aggregation induced by ADP or low concentrations of collagen was accompanied by inhibition of 5-hydroxytryptamine secretion. EC50 values were 10 and 9 [H9262]g/ml antibody against ADP and collagen induced responses respectively. In washed platelets treated with the cyclooxygenase inhibitor, indomethacin, PM6/13 inhibited platelet aggregation induced by thrombin (0.2 U/ml), collagen (10 [H9262]g/ml) and U46619 (3 [H9262]M) with EC50 = 4, 8 and 4 [H9262]g/ml respectively, without affecting [14C]5-hydroxytryptamine secretion or [3H]arachidonate release in appropriately labelled cells. Studies in Fura 2-labelled platelets revealed that elevation of intracellular calcium by ADP, thrombin or U46619 was unaffected by PM6/13 suggesting that the epitope recognised by the antibody did not influence Ca2+ regulation. In agreement with the results from the platelet aggregation studies, PM6/13 was found to potently inhibit binding of 125I-fibrinogen to ADP activated platelets. Binding of this ligand was also inhibited by two other MAbs tested, namely SZ-21 (also to GPIIIa) and PM6/248 (to the GPIIb-IIIa complex). However when tested against binding of 125I-fibronectin to thrombin stimulated platelets, PM6/13 was ineffective in contrast with SZ-21 and PM6/248, that were both potent inhibitors. This suggested that the epitopes recognised by PM6/13 and SZ-21 on GPIIIa were distinct. Studies employing proteolytic dissection of 125I-labelled GPIIIa by trypsin followed by immunoprecipitation with PM6/13 and analysis by SDS-PAGE, revealed the presence of four fragments at 70, 55, 30 and 28 kDa. PM6/13 did not recognize any protein bands on Western blots performed under reducing conditions. However Western blotting analysis with PM6/13 under non-reducing conditions revealed strong detection of the parent GP IIIa molecule, of trypsin treated samples revealed recognition of an 80 kDa fragment at 1 min, faint recognition of a 60 kDa fragment at 60 min and no recognition of any product at 18 h treatment. Under similar conditions, SZ-21 recognized fragments at 80, 75 and 55 kDa with the 55kDa species persisting even after 18 h trypsin treatment. These studies confirm the epitopes recognised by PM6/13 and SZ-21 to be distinct and that PM6/13 represents a useful tool to differentiate the characteristics of fibrinogen and fibronectin binding to the GPIIb-IIIa complex on activated platelets.

Sign in / Sign up

Export Citation Format

Share Document