Characterization of digestive proteases in the weevil Aubeonymus mariaefranciscae and effects of proteinase inhibitors on larval development and survival

ABSTRACT In the Southeast of Mexico, there are many native cichlids with commercial interest such as redhead cichlid (Vieja melanurus) and twoband cichlid (V. bifasciata), which have a great local demand and excellent meat quality. However, it is necessary to implement their culture based on nutrition studies and digestive biochemistry. This study’s objective was to characterize these two cichlids’ digestive proteases (pH, temperature, and inhibitors) through biochemistry techniques. Results showed that V. melanurus and V. bifasciata have a digestive capacity analogous to other omnivore fishes, where the optimal pH values of stomach proteases (4 and 2, respectively) and intestinal proteases (6 and 12, respectively), the optimal temperature of acid (35°C and 55°C, respectively) and alkaline proteases (45°C and 55°C, respectively) are quite similar. Both species presented high thermal and pH stabilities. Inhibition showed that V. melanurus is more sensitive to specific inhibitors for alkaline proteases than V. bifasciata. In conclusion, V. bisfasciata and V. melanurus have different digestive protease patterns. Both species can hydrolyze different protein ingredients to formulate a specific diet. Nevertheless, V. bifasciata is more resistant to the presence of inhibitors, which allow it to include vegetable proteins in its diet.

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Proteolytic activity in Plagiodera versicolora Laicharting (Coleoptera: Chrysomelidae): Characterization of digestive proteases and effect of host plants

Journal of Asia-Pacific Entomology ◽

10.1016/j.aspen.2013.04.007 ◽

2013 ◽

Vol 16 (3) ◽

pp. 329-334 ◽

Cited By ~ 2

Author(s):

Arash Zibaee ◽

Jalil Hajizadeh

Keyword(s):

Proteolytic Activity ◽

Host Plants ◽

Plagiodera Versicolora ◽

Digestive Proteases

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Acid-Stable Serine Proteinase Inhibitors in the Urine of Alzheimer Disease Subjects

Disease Markers ◽

10.1155/1996/193092 ◽

1996 ◽

Vol 13 (1) ◽

pp. 31-41 ◽

Cited By ~ 3

Author(s):

Giulia Sparro ◽

Salvatore Bonaiuto ◽

Gabriella Galoenzi ◽

Anna Maria Eleuteri ◽

Mauro Angeletti ◽

...

Keyword(s):

Proteinase Inhibitors ◽

Serine Proteinase ◽

Trypsin Inhibitors ◽

Urinary Trypsin Inhibitor ◽

Urinary Levels ◽

Urinary Acid ◽

Kallikrein Activity ◽

Acid Stable ◽

Kallikrein Inhibitors

A comparative study of the levels of acid-stable proteinase inhibitors (kallikrein and trypsin inhibitors) in the urine of healthy and Alzheimer subjects, of both sexes, has been performed. A preliminary characterization of the purified inhibitors indicates that the urinary antitryptic activity is accounted for by the presence of the well known Urinary Trypsin Inhibitor (UTI) while an apparently new molecule appears to be responsible for the anti kallikrein activity. The urinary levels of kallikrein inhibitors are very similar in healthy and sick subjects while the levels of trypsin inhibitors appear significatively increased in Alzheimer subjects of both sexes. The data presented here support the hypothesis that unpaired proteolytic processes could be involved in the pathogenesis of Alzheimer's disease and suggest that the levels of urinary acid-stable inhibitors may prove to be useful markers of the disease.

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Guinea Pig Plasma Trypsin Inhibitors. Purification and Characterization of two Functionally Distinct Proteinase Inhibitors

Biological Chemistry Hoppe-Seyler ◽

10.1515/bchm3.1992.373.1.43 ◽

1992 ◽

Vol 373 (1) ◽

pp. 43-50

Author(s):

Takahisa IMAMURA ◽

Takeshi KAMBARA

Keyword(s):

Guinea Pig ◽

Proteinase Inhibitors ◽

Trypsin Inhibitors ◽

Purification And Characterization

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Proteinase inhibitors in rat serum. Purification and partial characterization of three functionally distinct trypsin inhibitors

Biochemical Journal ◽

10.1042/bj2180953 ◽

1984 ◽

Vol 218 (3) ◽

pp. 953-959 ◽

Cited By ~ 15

Author(s):

L Kuehn ◽

M Rutschmann ◽

B Dahlmann ◽

H Reinauer

Keyword(s):

Proteinase Inhibitor ◽

Proteinase Inhibitors ◽

Serine Proteinase ◽

The Other ◽

Serine Proteinases ◽

Rat Serum ◽

Apparent Homogeneity ◽

Human Counterpart ◽

Proteinase Inhibitor Ii

Three different serine proteinase inhibitors were isolated from rat serum and purified to apparent homogeneity. One of the inhibitors appears to be homologous to alpha 1-proteinase inhibitor isolated from man and other species, but the other two, designated rat proteinase inhibitor I and rat proteinase inhibitor II, seem to have no human counterpart. alpha 1-Proteinase inhibitor (Mr 55000) inhibits trypsin, chymotrypsin and elastase, the three serine proteinases tested. Rat proteinase inhibitor I (Mr 66000) is active towards trypsin and chymotrypsin, but is inactive towards elastase. Rat proteinase inhibitor II (Mr 65000) is an effective inhibitor of trypsin only. Their contributions to the trypsin-inhibitory capacity of rat serum are about 68, 14 and 18% for alpha 1-proteinase inhibitor, rat proteinase inhibitor I and rat proteinase inhibitor II respectively.

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