Analysis of cultivable Porphyromonas gingivalis with trypsin-like protease enzyme activity and serum antibodies in chronic adult periodontitis

Oral Diseases ◽  
2008 ◽  
Vol 1 (2) ◽  
pp. 70-76 ◽  
Author(s):  
AJ Smith ◽  
WG Wade ◽  
J Greenman ◽  
M Addy
2000 ◽  
Vol 57 (6) ◽  
pp. 1113-1119 ◽  
Author(s):  
James C Smoot ◽  
Robert H Findlay

Measuring digestive enzyme and surfactant activities tested specialization of gizzard shad (Dorosoma cepedianum) digestive physiology to a detritivorous feeding strategy. Digestive enzyme activity was measured in adult and larval gizzard shad using fluorescently labeled artificial substrates. Surfactant activity in gizzard shad was measured by comparing gut juice drop diameters over a range of dilutions. Enzyme activity in the ceca region of adult gizzard shad was high for esterase, beta-glucosidase, lipase, and protease. Enzyme activity was lower in posterior intestine sections than in anterior intestine sections, although protease activity remained high for the greatest distance in the intestine. Micelles were detected in adult gizzard shad gut juice, and surfactant activity was greatest in the ceca region. Larval gizzard shad protease activity was similar to that of adult fish, and surfactants were below their critical micelle concentration. Gizzard shad coupled digestive physiology with gut anatomy to obtain nutrients from detritus, and these adaptations may explain elevated growth rates observed in these fish when they are planktivorous.


Toxicon ◽  
1979 ◽  
Vol 17 (6) ◽  
pp. 529-537 ◽  
Author(s):  
Yaw-Shong Jong ◽  
B.R. Norment ◽  
James R. Heitz

2021 ◽  
Vol 11 ◽  
Author(s):  
Noémi Bencze ◽  
Csaba Schvarcz ◽  
Gábor Kriszta ◽  
Lea Danics ◽  
Éva Szőke ◽  
...  

There is growing interest in the role of nerve-driven mechanisms in tumorigenesis and tumor growth. Capsaicin-sensitive afferents have been previously shown to possess antitumoral and immune-regulatory properties, the mechanism of which is currently poorly understood. In this study, we have assessed the role of these terminals in the triple negative 4T1 orthotopic mouse model of breast cancer. The ultrapotent capsaicin-analogue resiniferatoxin (RTX) was used for the selective, systemic desensitization of capsaicin-sensitive afferents. Growth and viability of orthotopically implanted 4T1 tumors were measured by caliper, in vivo MRI, and bioluminescence imaging, while tumor vascularity and protease enzyme activity were assessed using fluorescent in vivo imaging. The levels of the neuropeptides Calcitonin Gene-Related Peptide (CGRP), Substance P (SP), and somatostatin were measured from tumor tissue homogenates using radioimmunoassay, while tumor structure and peritumoral inflammation were evaluated by conventional use of CD31, CD45 and CD3 immunohistology. RTX-pretreated mice demonstrated facilitated tumor growth in the early phase measured using a caliper, which was coupled with increased tumor vascular leakage demonstrated using fluorescent vascular imaging. The tumor size difference dissipated by day seven. The MRI tumor volume was similar, while the intratumoral protease enzyme activity measured by fluorescence imaging was also comparable in RTX-pretreated and non-pretreated animals. Tumor viability or immunohistopathological profile was measured using CD3, CD31, and CD45 stains and did not differ significantly from the non-pretreated control group. Intratumoral somatostatin, CGRP, and SP levels were similar in both groups. Our results underscore the beneficial, antitumoral properties of capsaicin sensitive nerve terminals in this aggressive model of breast cancer, which is presumed to be due to the inhibition of tumor vascular bed disruption. The absence of any difference in intratumoral neuropeptide levels indicates non-neural sources playing a substantial part in their expression.


2021 ◽  
Vol 42 (4(SI)) ◽  
pp. 1195-1200
Author(s):  
S. Thirukkumar ◽  
◽  
G. Hemalatha ◽  
S. Vellaikumar ◽  
M. Murugan ◽  
...  

Aim: This research aimed to optimize suitable hydrolytic enzymes for maximizing cottonseed milk extracts for high cottonseed milk yield, protein content and low gossypol level. Methodology: Known amount of cottonseed was soaked for 90 min at 32°C and blended (cottonseed:water@1:6). Different aliquots of the blended cottonseed slurry were treated with 1% of enzymes viz., protease, cellulase and α-amylase enzyme at pH 7.0 followed by incubation at 40 and 52°C for 2.30 hr for the extraction of cottonseed milk. The enzyme activity of extracted milk was subsequently inactivated by pasteurization (90°C, 5 min). Further analysis of physico-chemical characteristics was also carried. The control sample included milk extraction from non-enzyme treated cottonseed milk extract (30±2°C). Results: Among different treatments, cottonseed milk extraction using protease enzyme at 40°C incubation showed the highest milk yield (86.71%) with the lowest sedimentation (3.72%). Further incubation 40°C and 52°C showed the highest protein content of 2.10 and 2.27 g 100 ml-1 and gossypol reduction of 40.36 and 35.22%, respectively, in the cottonseed milk extract. Meanwhile, cellulase and α-amylase enzymes treated samples at both incubation temperatures showed poor physico-chemical characteristics as compared to control. Interpretation: Protease enzyme seems to be the most suitable for optimum or higher extraction of cottonseed milk.


2019 ◽  
Vol 6 ◽  
pp. 113-118 ◽  
Author(s):  
Karuna Neupane ◽  
Rama Khadka

Objectives: To evaluate the enzymatic and antimicrobial efficacy of enzyme from garbage produced from different fruits and vegetable wastes. Methods: This study was conducted from October-2018 to February-2019 in the laboratory of Padma Kanya Multiple College, Bagbazar, Kathmandu, Nepal. This study was carried for production, analysis of enzymatic and antimicrobial efficacy by using yeast (Saccharomyces cerevisae) and bacteria (Bacillus species) in 5 fruits peels, Mosambi (Citrus limetta), Pomegranate (Punica granatum), Pineapple (Ananas comosus), Papaya (Carica papaya) and mixed fruits collected from fresh fruit stall and vegetable peels collected from college’s hostel. The fermentation mixture was made in the ratio 1:3:10 (1 part brown sugar, 3 parts fruits/vegetable peels and 10 parts water) and left for 3 months for fermentation. Results: After fermentation, enzyme activity (amylase, protease, caseinase, cellulase and lipase) and antimicrobial efficacy (S. aureus, S. aureus (ATCC 25923), Bacillus spp, Salmonella Typhi, E. coli, E. coli (ATCC 25922), Shigella spp, Pseudomonas aeruginosa) were analyzed. All the samples showed amylase and caseinase enzyme activity, only Pineapple (Ananascomosus), Papaya (Carica papaya) and Mixed fruit showed protease enzyme activity while only Pomegranate (Punicagranatum) showed lipase enzyme activity. In antimicrobial efficacy test, garbage enzyme produced from vegetable sample didn’t show antimicrobial activity with bacteria used except E. coli (ATCC 25922)and S. aureus (ATCC 25923). Similarly, garbage enzyme produced from Mixed fruit and Papaya (Carica papaya) didn’t show antimicrobial activity with Salmonella Typhi and S. aureus (ATCC 25923) respectively but garbage enzyme from other wastes showed antimicrobial activity with bacteria used in test. Conclusion: Different fruits and vegetables wastes showed different enzyme activity and antimicrobial activity.


2013 ◽  
Vol 11 (4) ◽  
pp. 291-299
Author(s):  
Mio Hagiwara ◽  
Tomoko Kurita-Ochiai ◽  
Tomomi Hashizume-Takizawa ◽  
Masaaki Suemitsu ◽  
Kayo Kuyama ◽  
...  

2019 ◽  
Vol 16 (04) ◽  
pp. 817-826
Author(s):  
Endang Rahmawati ◽  
Abinawanto Abinawanto ◽  
Is Helianti

ABSTRACT: Proteases are potential enzymes that utilized in various industrial fields, and the demand of these enzymes is increasing. Bacillus halodurans CM1 is Indonesia indigenous bacterium which is detected to be able to produce alkalotermophilic protease enzyme. In this study, we subcloned the protease gene consist of Open Reading Frame of protease gene and its promoter from Bacillus halodurans CM1 in Bacillus subtilis DB104 via conjugation, and analyzed the expression of the recombinant protease. The protease gene is 1 417 bp length including the open reading frame and the promoter, and obtained by PCR and cloned into pGEM T easy. After confirmed by sequencing, the gene was subcloned into vector pBBRE194, then the recombinant plasmid was transformed into E. coli S17-1. This E.coli was then conjugated to Bacillus subtilis DB104. The target recombinant B. subtilis DB104 has been obtained confirmed by plasmid verification and erythromycin resistance. The recombinant protease produced showed the highest enzyme activity at 50oC and pH 9 (with pH range 5-9) which with protease activity 13.66 U/mL.


2018 ◽  
Vol 13 (2) ◽  
pp. 209-216
Author(s):  
Dyah Hesti Wardhani ◽  
Bakti Jos ◽  
Abdullah Abdullah ◽  
Suherman Suherman ◽  
Heri Cahyono

Cheese is one of the popular dairy products with high nutrient content. Coagulation as an important process in making cheese, wherein, the curd will be separated from the milk whey. This coagulation can use the enzyme rennet, acid, or a combination of both. This study aims to study the effect of coagulant agents on yield, protease enzyme activity, and curd texture on cheese making. Coagulant agents used are acetic acid, citric acid, lime and lemon combined with the enzyme rennet. The process begins with pasteurized milk and analyzed, the milk is pasteurized and analyzed first to obtain moisture content, density and pH. The coagulant added is 25-45% with a base of 50 ml of milk and 5 mL of the enzyme rennet. The curd formed is then separated from the whey using a filter cloth and analyzed for its water content and pH. The coagulant of acetic acid and citric acid produced a higher yield curd of 94.66% (4% acetic acid) and 93.9% (5% citric acid) compared to the highest yield of curd that can be produced by lime and lemon coagulant which is 68 72% (lemon orange 45%) and 61.84% (lime 45%). The texture of the curd formed by lime and lemon juice is more fragile than the curd texture with coagulant of acetic acid and citric acid. Each coagulant provides a diverse response to protease enzyme activity.


2020 ◽  
Vol 09 ◽  
Author(s):  
Shirin Saberianpour ◽  
Leila Abkhooie ◽  
Babak Elyasifar ◽  
Azita Dilmaghani

Background : Proteases are the most important industrial enzymes with diverse applications in. Bacteria, such as Bacillus, commonly used to produce protease for industrial purposes. Proteases are commercially exploited in large-scale, especially in pharmaceutical, food, leather and detergent industries. Objective: The aim of this study was screening and optimization of protease enzyme activity produced by local bacteria. Method: In this research, the effect of incubation time, temperature and initial pH were investigated to improve the extracellular protease enzyme activity by two bacteria, named Bacillus subtilis strain DAR and Alkalihalobacillus hwajinpoensis strain 3NB. These two isolates have already been isolated and registered from Iran. Results: The results indicated that the optimum incubation time for protease activity in B. subtilis strain DAR is 36 h in contrast to 40 h in Alkalihalobacillus hwajinpoensis strain 3NB. The optimum incubation temperatures for enzyme activity for B. subtilis and Alkalihalobacillus hwajinpoensis is 50°C and 40°C, respectively. Optimum pH conditions for protease activity for both of the bacteria is 8. Conclusion: In current study, we investigated the optimum incubation time, pH and temperature for best protease activity. Further studies are recommended to improve protease activity through changing enzyme substrates.


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