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

2013 ◽  
Vol 16 (3) ◽  
pp. 329-334 ◽  
Author(s):  
Arash Zibaee ◽  
Jalil Hajizadeh
Keyword(s):  
Proteolytic Activity ◽  
Host Plants ◽  
Plagiodera Versicolora ◽  
Digestive Proteases

scholarly journals Characterization of Ficus benjamina and Artocarpus heterophyllus Proteases as Potential Rennet Alternatives

2020 ◽  
Vol 12 (2) ◽  
pp. 213-219
Author(s):  
Andreas Binar Aji Sukmana ◽  
Indy Widyaningrum ◽  
Rischa Karmila Lani ◽  
Sri Kasmiyati
Keyword(s):  
Proteolytic Activity ◽  
Scientific Knowledge ◽  
Knowledge Development ◽  
Small Scale ◽  
Optimum Conditions ◽  
Artocarpus Heterophyllus ◽  
Ficus Benjamina ◽  
Crucial Component ◽  
Plant Proteases

Rennet, a milk coagulant exhibiting proteolytic activity, is a crucial component in cheese industries. Its price and availability have discouraged the growth of some small scale cheese industries. Therefore, an alternative for rennet will be beneficial for the industries. Among other sources, plant proteases offer some advantages as rennet alternatives. This study aimed to investigate the potential of plant proteases obtained from the latex as potential rennet alternatives. A total of six plants from the genus Ficus and Artocarpus were screened for their proteolytic activity and milk coagulating ability. The screening indicated that all six tested plants displayed proteolytic activity at various levels, but only Ficus benjamina and Artocarpus heterophyllus produced a firm milk curd. Hence, both F. benjamina and A. heterophyllus were determined to be the most potential. Further characterizations suggested that F. benjamina and A. heterophyllus protease were optimum at pH 7.0 also at 50°C and 40°C, respectively. At their optimum conditions, both proteases exhibited a lower MCA/PA ratio than that of the rennet. This study contributed to scientific knowledge development by becoming the first to characterize the optimum conditions of F. benjamina and A. heterophyllus’ proteases, investigate their MCA/PA ratio, and compare their activity against commercial rennet. The examination of their potentials as rennet alternatives could benefit small cheese industries and the communities.

Characterization of proteolytic and anti-proteolytic activity involvement in sterlet spermatozoon maturation

2016 ◽  
Vol 42 (6) ◽  
pp. 1755-1766 ◽  
Author(s):  
Viktoriya Dzyuba ◽  
Mariola Słowińska ◽  
Jacky Cosson ◽  
Andrzej Ciereszko ◽  
Sergii Boryshpolets ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Activity Involvement

scholarly journals Characterization of 16- to 20-Kilodalton (kDa) Connective Tissue Growth Factors (CTGFs) and Demonstration of Proteolytic Activity for 38-kDa CTGF in Pig Uterine Luminal Flushings1

1998 ◽  
Vol 59 (4) ◽  
pp. 828-835 ◽  
Author(s):  
DeAnna K. Ball ◽  
Gulnar A. Surveyor ◽  
John R. Diehl ◽  
Christy L. Steffen ◽  
Mehmet Uzumcu ◽  
...  
Keyword(s):  
Growth Factors ◽  
Connective Tissue ◽  
Proteolytic Activity ◽  
Tissue Growth

Partial characterization of digestive proteases in tropical gar Atractosteus tropicus juveniles

2013 ◽  
Author(s):  
R. Guerrero-Zárate ◽  
C. A. Alvarez-González ◽  
M. A. Olvera-Novoa ◽  
N. Perales-García ◽  
C. A. Frías-Quintana ◽  
...  
Keyword(s):  
Partial Characterization ◽  
Digestive Proteases ◽  
Tropical Gar ◽  
Atractosteus Tropicus

Comparative characterization of digestive proteases in redhead cichlid (Vieja melanurus) and twoband cichlid (Vieja bifasciata) (Percoidei: Cichlidae)

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Carlos Alfonso Frías-Quintana ◽  
Emyr Saul Peña-Marín ◽  
Carlos David Ramírez-Custodio ◽  
Rafael Martínez-García ◽  
Luis Daniel Jiménez-Martínez ◽  
...  
Keyword(s):  
Meat Quality ◽  
Alkaline Proteases ◽  
Optimal Temperature ◽  
Digestive Capacity ◽  
Digestive Proteases ◽  
Ph Values ◽  
Specific Diet ◽  
Specific Inhibitors ◽  
Optimal Ph

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.

scholarly journals Characterization of the soluble, secreted form of urinary meprin

1996 ◽  
Vol 315 (2) ◽  
pp. 461-465 ◽  
Author(s):  
Robert J. BEYNON ◽  
Simon OLIVER ◽  
Duncan H. L. ROBERTSON
Keyword(s):  
Proteolytic Activity ◽  
Protein Band ◽  
Peptide Sequence ◽  
Soluble Form ◽  
Α Subunit ◽  
Alternative Processing ◽  
Sds Page ◽  
Processing Pathways ◽  
Membrane Bound

A soluble form of the kidney membrane metalloendopeptidase, meprin, is present in urine. Urinary meprin is expressed in BALB/C mice with the Mep-1a/a genotype (high meprin, expressing meprin-α and meprin-β) but not in BALB.K mice of the Mep-1b/b genotype (that only express meprin-β). Western blotting with antisera specific to the meprin-α and the meprin-β subunits established that the only form of meprin present in urine samples was derived from meprin-α. This form of meprin is partially active, and comprises at least three variants by non-reducing SDS/PAGE and by zymography and two protein bands on reducing SDS/PAGE. Sequencing of these two bands established that the N-terminus of the larger protein band begins with the pro-peptide sequence of the α-subunit (VSIKH..), whereas the smaller band possessed the mature meprin N-terminal sequence (NAMRDP..). Trypsin is able to remove the pro-peptide, with a concomitant activation in proteolytic activity. After deglycosylation, the size of the pro- and mature forms of urinary meprin are consistent with cleavage in the region of the X–I boundary. There is a pronounced sexual dimorphism in urinary meprin expression. Females secrete a slightly larger form, and its proteolytic activity is about 50% of that released by males. The urinary meprin is therefore a naturally occurring secreted form of this membrane-bound metalloendopeptidase and is more likely to be generated by alternative processing pathways than by specific release mechanisms.

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