An advance for removing antinutritional protease inhibitors: Soybean whey purification of Bowman-Birk chymotrypsin inhibitor by combination of two oppositely charged polysaccharides

2017 ◽  
Vol 164 ◽  
pp. 349-357 ◽  
Author(s):  
Xingfei Li ◽  
Yufei Hua ◽  
Yeming Chen ◽  
Xiangzhen Kong ◽  
Caimeng Zhang ◽  
...  
2012 ◽  
Vol 8 (12) ◽  
pp. 3335 ◽  
Author(s):  
Francesca Tedeschi ◽  
Antimo Di Maro ◽  
Angelo Facchiano ◽  
Susan Costantini ◽  
Angela Chambery ◽  
...  

2012 ◽  
Vol 52 (3) ◽  
pp. 368-373 ◽  
Author(s):  
Maryam Ajamhassani ◽  
Arash Zibaee ◽  
Jalal Sendi ◽  
Hassan Askary ◽  
Nasser Farrar

Proteolytic Activity in the Midgut of the Crimson Speckled MothUtethesia PulchellaL. (Lepidoptera: Arctiidae)Samples were prepared from the midgut of 4th instar larvae of the crimson speckled mothUtethesia pulchellaL. to find proteolytic activity and properties. Result revealed the presence of high proteolytic activity in the midgut when taking into account specific proteinases including trypsin-like, chymotrypsin-like, elastase and two exopeptidase (aminopeptidase and carboxipeptidase). The optimal pH of general protease was 8 and 7 when using azocasein and hemoglobin as general substrates, respectively. The optimal temperature of the total proteolytic activity in the midgut ofU. pulchellawas 25°C and 30°C when using azocasein and hemoglobin, respectively. Proteolytic activity was inhibited significantly by soybean trypsin inhibitor (SBTI), phenylmethylsulfonyl fluoride (PMSF), trypsin inhibitor (TLCK), chymotrypsin inhibitor (TPCK) and Phenanthroline. These results provide evidences for the presence of serine proteinases as the major proteases in the midgut ofU. pulchella;a key rangeland pest in warm climates. The interaction between digestive proteases and protease inhibitors have potentially important consequences for pest management programs.


Foods ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 415 ◽  
Author(s):  
Claudia Arribas ◽  
Blanca Cabellos ◽  
Carmen Cuadrado ◽  
Eva Guillamón ◽  
Mercedes M. Pedrosa

Pasta is considered as the ideal vehicle for fortification; thus, different formulations of gluten-free pasta have been developed (rice 0–100%, bean 0–100%, and carob fruit 0% or 10%). In this article, the content of individual inositol phosphates, soluble sugars and α-galactosides, protease inhibitors, lectin, phenolic composition, color, and texture were determined in uncooked and cooked pasta. The highest total inositol phosphates and protease inhibitors contents were found in the samples with a higher bean percentage. After cooking, the content of total inositol phosphates ranged from 2.12 to 7.97 mg/g (phytic acid or inositol hexaphosphate (IP6) was the major isoform found); the protease inhibitor activities showed values up to 12.12 trypsin inhibitor (TIU)/mg and 16.62 chymotrypsin inhibitor (CIU)/mg, whereas the competitive enzyme-linked immunosorbent assay (ELISA) showed the elimination of lectins. Considering the different α-galactosides analyzed, their content was reduced up to 70% (p < 0.05) by the cooking process. The total phenols content was reduced around 17–48% after cooking. The cooked samples fortified with 10% carob fruit resulted in darker fettuccine with good firmness and hardness and higher antioxidant activity, sucrose, and total phenols content than the corresponding counterparts without this flour. All of the experimental fettuccine can be considered as functional and healthy pasta mainly due to their bioactive compound content, compared to the commercial rice pasta.


Author(s):  
S.W. French ◽  
N.C. Benson ◽  
C. Davis-Scibienski

Previous SEM studies of liver cytoskeletal elements have encountered technical difficulties such as variable metal coating and heat damage which occurs during metal deposition. The majority of studies involving evaluation of the cell cytoskeleton have been limited to cells which could be isolated, maintained in culture as a monolayer and thus easily extracted. Detergent extraction of excised tissue by immersion has often been unsatisfactory beyond the depth of several cells. These disadvantages have been avoided in the present study. Whole C3H mouse livers were perfused in situ with 0.5% Triton X-100 in a modified Jahn's buffer including protease inhibitors. Perfusion was continued for 1 to 2 hours at ambient temperature. The liver was then perfused with a 2% buffered gluteraldehyde solution. Liver samples including spontaneous tumors were then maintained in buffered gluteraldehyde for 2 hours. Samples were processed for SEM and TEM using the modified thicarbohydrazide procedure of Malich and Wilson, cryofractured, and critical point dried (CPD). Some samples were mechanically fractured after CPD.


1975 ◽  
Vol 34 (03) ◽  
pp. 763-769
Author(s):  
K Worowski

SummaryThe potato protease inhibitors inhibit intrinsic prothrombin activators and trypsin activation of prothrombin. The inhibitors 5a and 5b are responsible for the intrinsic prothrombin activator inhibition. This inhibition is progressive. No inhibition by these inhibitors of tissue thromboplastin activation of prothrombin or thrombin activity was observed.


Sign in / Sign up

Export Citation Format

Share Document