scholarly journals Water-soluble protein molecular weight distribution and effects on wheat malt quality during malting

2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
Lan Xie ◽  
Yuhong Jin ◽  
Jinhua Du ◽  
Kaili Zhang
Keyword(s):  
Molecular Weight ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Soluble Protein ◽  
Water Soluble ◽  
Malt Quality ◽  
Water Soluble Protein ◽  
Protein Molecular Weight

scholarly journals Studies on silk proteins I. The properties and constitution of fibroin. The conversion of fibroin into a water-soluble form and its bearing on the phenomenon of denaturation

1947 ◽  
Vol 190 (1021) ◽  
pp. 145-169 ◽  
Keyword(s):  
Molecular Weight ◽  
Soluble Protein ◽  
Optical Rotation ◽  
Amino Nitrogen ◽  
Water Soluble ◽  
Soluble Form ◽  
Secondary Process ◽  
Amide Nitrogen ◽  
Water Soluble Protein ◽  
The Mean

Some of the constituent amino-acids of fibroin (degummed silk) are determined. Special attention is directed to histidine, owing to its use in the calculation of the molecular weight of fibroin. A value of 0⋅45% has been found by methods in which the histidine is isolated as nitranilate or di-(3:4-dichlorobenzenesulphonate). Other values obtained are serine 12⋅6%, threonine 1⋅5%, tyrosine 10⋅6%, and proline 1⋅5%. Hydroxyproline appears to be absent, but the presence of small amounts of some hydroxyamino-acid other than serine and threonine is indicated. The mean residue weight of fibroin is determined by three methods, one of which is a new method based on analysis of the complex formed between fibroin and cupri-ethylenediamine. This method gives a Cu:fibroin-N ratio of 1:1⋅92 and, if allowance is made for co-ordination with the tyrosine hydroxy1 group, an equivalence of 1⋅964 atoms of peptide-nitrogen to 1 atom of copper is obtained. The three methods give an average value of 78⋅0 for the mean residue weight of fibroin. This value, together with the most acceptable data for amino-acid constituents, indicate that the unidentified anhydro-residues (about 20%) have a mean residue weight of about 107. Evidence is presented that fibroin contains no amide-nitrogen. Methods for the determination of amide-nitrogen at present in use, which indicate a content of 1 to 2%, are considered to be unreliable. Fibroin dissolved in cupri-ethylenediamine gives, on neutralization and dialysis of the resulting solution, a water-soluble protein. The production of this water-soluble protein is attended by little or no degradation of the original fibroin as shown by determinations of fluidity, amino-nitrogen, and acid- and alkali-combining power. The water-soluble protein is precipitated by the normal protein-precipitating reagents, but in every instance examined the precipitated material exhibits an insolubility comparable with that of the original fibroin. Factors responsible for the solubilization process are investigated and data for molecular weight, titration values, ultra-violet absorption spectra, reducing activity, optical rotation, tryptic hydrolysis, and viscosity for both soluble and dispersed fibroin are given. Soluble fibroin has [ α ] D 15 — 53⋅1° and dispersed fibroin [ α ] D 15 — 58⋅9°, both in aqueous media. The preparation and properties of films and filaments of fibroin are described. Films of fibroin can be prepared that are water-soluble. On stretching, these films show strain-birefringence, acquire considerable tensile strength, and become insoluble in water, but X-ray examination gives the β -keratin pattern for both the stretched and unstretched films. Reasons are advanced for considering the water-soluble form of fibroin to be the native or renatured protein and the original protein to be the denatured form. The denaturation of fibroin is discussed on the basis that denaturation is essentially an unfolding of a coiled long-chain molecule. The subsequent aggregation of the uncoiled molecules to give an insoluble product is considered to be a secondary process. Some aspects of protein and polypeptide chains as macro-molecules are also discussed.

A comparison of the storage protein (globulin) of eight species of Cucurbitaceae

1979 ◽  
Vol 57 (19) ◽  
pp. 2044-2049 ◽  
Author(s):  
Brendan T. O'Kennedy ◽  
Charles C. Reilly ◽  
John S. Titus ◽  
Walter E. Splittstoesser
Keyword(s):  
Molecular Weight ◽  
Soluble Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Basic Structure ◽  
Water Soluble ◽  
Molecular Weights ◽  
Heat Stable ◽  
Water Soluble Protein ◽  
Cucurbitaceae Family

The percentage of globulin from cotyledons of dormant seeds of eight species of the Cucurbitaceae family was similar. After 4 days of germination, the globulin fraction decreased with a concomitant increase in the water-soluble protein fraction. Small changes in total protein occurred. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis showed that the globulins of the eight species were composed of high molecular weight proteins which were different. The subunit arrangement of the globulin suggests a tetramer structure with a molecular weight greater than 200 000. After4 days of germination, a heat-stable, water-soluble protein was produced from the globulin. When this protein was reduced with β-mercaptoethanol, followed by electrophoresis, two peptides with molecular weights of 18 500 and 20 000 were produced in each species. It was concluded that all of the globulins have the same basic structure in different subunit arrangements.

scholarly journals The Potential of Hydrolysate from Rabbit Meat Protein as an Angiotensin Converting Enzyme Inhibitor

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Edy Permadi ◽  
Jamhari Jamhari ◽  
Edi Suryanto ◽  
Zaenal Bachruddin ◽  
Yuny Erwanto
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Soluble Protein ◽  
Ace Inhibitor ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Soluble Protein Content ◽  
Water Soluble Protein ◽  
Rabbit Meat ◽  
Ace Inhibitory

This research aimed to investigate the rabbit meat hydrolysate potential as an angiotensin-converting enzyme (ACE) inhibitor. Indonesian local rabbit meats were used in this study. The research was conducted in Department of Animal Product Technology, Faculty of Animal Science, Universitas Gadjah Mada, from August 2016 to February 2017. The local rabbit meats were hydrolyzed by pepsin, trypsin, and pancreatic. The obtained hydrolysates were then analyzed to identify the water-soluble protein content. The molecular weight of the hydrolysates were also confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The ACE inhibitory properties of the hydrolysates were analyzed in vitro. The results showed that pepsin, trypsin, and pancreatic hydrolysis showed a significant effect on the water-soluble protein content of rabbit meat (p<0.05). The water-soluble protein of rabbit meat hydrolysed by pepsin, trypsin, and pancreatic were 9.41, 7.66, and 9.75 mg/mL respectively. The molecular weight of the rabbit meat hydrolysate were increased from 10 to 43 kDa; 17 to 43 kDa; and 10 to 43 kDa, after hydrolysed by by pepsin, trypsin, and pancreatic respectively. Furthermore, the ACE inhibitory properties ) of the hydrolysed rabbit meat by pepsin, trypsin, and pancreatic were 439, 170, and 380 μg/mL, respectively. The rabbit meat hydrolysate showed a potential to be ACE inhibitor after hydrolyzed with pepsin, trypsin and pancreatic. Moreover, it also showed a promising potential to be used as bioactive components in different pharmaceutical applications. The highest ACE inhibitory capability was showed on trypsin hydrolysis with the total of 65.45% and 170 μg/mL ACE inhibition

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