scholarly journals Protease production and enzymatic soaking of salt-preserved buffalo hides for leather processing

IIOAB Letters ◽  
2014 ◽  
Vol 3 (1) ◽  
Author(s):  
V. P. Zambare ◽  
S. S. Nilegaonkar ◽  
P. P. Kanekar
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Enzyme ◽  
Processing Time ◽  
Enzyme Concentration ◽  
Protease Production ◽  
Water Penetration ◽  
Leather Processing ◽  
Protease Enzyme ◽  
Rsm Optimization ◽  
Hydrolysis Of

Response surface methodological (RSM) optimization of protease by Pseudomonas aeruginosa MCM B327, increased 1.3-fold activity with 1% inoculum having cell density of 27.57 x 109 cells mL-1 at pH 7, 300C and 72 h of incubation. Protease enzyme recovered from P. aeruginosa showed characteristic activities against diverse proteins of hide. Enzyme was found to be active with substrates e.g. casein, Bovine serum albumin, gelatin, elastin, haemoglobin but inactive against keratin and collagen. During leather manufacturing, non-collagenase and non-keratinase activities have advantageous in a quality leather and hair saving process, respectively. Increased proteolytic enzyme concentration (0.1-0.5%) in soaking process showed increased water penetration because of hydrolysis of albumin and elastin proteins as indicated by opened fibers in histopathological sections. These findings suggest, protease secreted by P. aeruginosa may have application in soaking operation of leather processing for minimizing harmful deharing chemicals and processing time.

scholarly journals Extraction of Protease Under Solid State Fermentation using Bacterial Isolates from Traditional Leather Processing Waste Water Found Around Wukro Maray

2018 ◽  
Vol 15 (3) ◽  
pp. 509-515 ◽  
Author(s):  
Girma Haile ◽  
Birhanu Babiye
Keyword(s):  
Waste Water ◽  
Energy Consumption ◽  
Solid State ◽  
Wheat Bran ◽  
Bacterial Isolates ◽  
Processing Waste ◽  
Leather Processing ◽  
Protease Enzyme ◽  
Potential Activity ◽  
Hydrolysis Of

Enzymes are important in reducing both energy consumption and combating environmental pollution. Proteases are enzymes which catalyze the hydrolysis of protein molecules.Most of the tannery industries in Ethiopia use chemicals for dehairing that led great environmental and human health problem. The objectives of the present study were,to isolate potential protease producing bacteria from water sample collected from traditional leather processing waste water around Wukro maray;to extract the protease enzyme through SSF using cheap wheat bran, and evaluate the potential activity of the enzyme in leather dehairing. Water samples were serially diluted and 1ml of sample was spread on nutrient agar and kept at 370C for 24 hrs. Many colonies of bacteria were formed. The colony from C10-4 and G10-3 were taken by using inoculating loop for sub culturing to get pure colony. Then the pure cultured colony were inoculated into the 250 ml Erlenmeyer flasks containing substrate were fermented after 6 days incubation at 370C. The results of the unknown concentration of the crude protease enzyme showed successfully used as dehairing agent on hide. The results indicate that these bacteria isolate can be used as biotechnological tool for industrial purpose.

Micro-roughening of polyamide fabric using protease enzyme for improving adhesion strength of rubber-polyamide composite

2017 ◽  
Vol 37 (3) ◽  
pp. 297-306 ◽  
Author(s):  
S. Periyasamy ◽  
G. Krishna Prasad ◽  
Sajal Kumar Chattopadhyay ◽  
A.S.M. Raja ◽  
K. Raj Kumar ◽  
...  
Keyword(s):  
Surface Roughness ◽  
Adhesion Strength ◽  
Hydrolytic Degradation ◽  
Peel Strength ◽  
Enzyme Concentration ◽  
Enzyme Treatment ◽  
Sem Images ◽  
Protease Enzyme ◽  
Nylon 6,6 ◽  
Hydrolysis Of

Abstract The adhesion between rubber and the reinforcing textile plays an important role in ensuring the serviceability of composites. The present study aims to develop an enzyme based surface roughening process for nylon 6,6 fabric to improve its adhesion strength to rubber. Polyamide (nylon 6,6) fabric was micro-roughened through catalysed hydrolytic degradation of the surface chains, using a protease enzyme treatment. The concentration of the enzyme was optimized in terms of surface roughness measured by a KES-FB4 surface tester. Scanning electron microscopy (SEM) images of the protease treated fabric showed a heterogeneous rough appearance with cracks and pits. Fourier transform infrared (FTIR) analysis confirmed the surface hydrolysis of polyamide-6,6 due to the enzymatic treatment. Protease enzyme treated fabrics were then subjected to resorcinol formaldehyde latex (RFL) treatment, followed by a rubber moulding. Micro-roughening of nylon 6,6 fibre with an optimum surface roughness (SMD) of 20.3 μm was obtained for 3% enzyme concentration. Physicochemical mechanisms of the optimum effect and enzyme assisted hydrolysis were proposed. In line with surface roughness, peel strength also increased up to an enzyme concentration of 3% and then it decreased, however, the enzyme treated fabric showed higher peel strength than the control fabric.

scholarly journals Immobilization of Pseudomonas Aeruginosa in Different Matrices for the Production of Alkaline Protease

2020 ◽  
Vol 9 (1) ◽  
pp. 956-959
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Enzymatic Activity ◽  
Alkaline Protease ◽  
Calcium Alginate ◽  
Protease Production ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Microbial Cells ◽  
Protease Enzyme

Numerous enzymes are used in various types of industries, and one such enzyme used in several of these industries is proteases. Aforementioned, industries such as dairy, detergent, leather, fermentation and several other industries are benefitted with protease enzyme. In the present study, the efficiency of protease production was studied by enriching and immobilizing several matrices by a gram negative bacteria known as Pseudomonas aeruginosa .The immobilization was carried out by four different matrices under two different concentrations of 3% and 4%.Yielded results revealed highest enzymatic activity of 240 (U/ml) in 3% calcium alginate. Still, second highest enzymatic activity of 230 (U/ml) was seen in 4% calcium alginate. On the contrary, free microbial cells showed an enzymatic activity of 100 (U/ml). The peak activities for other methods area as follows: 4% calcium alginate - 133 (U/ml), 3% agar-agar - 100 (U/ml), 4% agar-agar - 91 (U/ml), 3% Gelatin - 85 (U/ml), 4% Gelatin - 88 (U/ml) and Polyacrylamide – 104 (U/ml). The most optimum matrix for the cellular entrapment of Pseudomonas aeruginosa is seen in 3% calcium alginate for alkaline protease production.

scholarly journals The effectiveness of Proteolytic bacteria in the leather and detergent industry isolated waste from the Modjo tannery

2021 ◽  
Author(s):  
Tayachew Desalegn ◽  
◽  
Ketema Bacha ◽  
Mesfin Tafesse ◽  
Chandran Masi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Proteolytic Enzymes ◽  
Digestive Enzyme ◽  
Total Solid ◽  
Growth Conditions ◽  
Protease Production ◽  
Alkaline Proteases ◽  
Extracellular Proteases ◽  
Protease Enzyme

Protease also called proteinase or peptidase is a digestive enzyme that is categorized under proteolytic enzymes and it has great potential in industrial application. Extracellular proteases are used in a variety of industries because they exhibit practically all of the characteristics needed for biotech applications such as detergent, bioremediation, food, and leather processing. In the synthesis of all three major types of acidic, neutral, and alkaline proteases, microbial sources have dominated an unbeatable area. Alkaline proteases are a large group of industrial enzymes formed by a wide variety of species, including animals, fungi, and bacteria. The fermentation method serves to make bacteria, fungi, and yeast alkaline proteases. Proteases are produced in large quantities by Gram-positive bacteria, especially those belonging to the Bacillus genus. Following standard procedures, the bacterial isolates PMOJ-01 and PMOJ-05 with the prominent zone of clearance and efficient enzyme development were further characterized to the genus level. Moreover, the growth conditions for the highest protease production were optimized with different pH, temperatures, and NaCl concentrations, in the results of PMOJ-01 and PMOJ- 05 pH (7 and 8), temperatures 45oC, and 1% NaCl concentrations both cases respectively. The proteases activities from PMOJ-01, Pseudomonas aeruginosa, and PMOJ-05, Bacillus subtilis were most active at pH 7.0 and pH 8.0 and temperature at 35oC and 45oC, respectively. The enzyme activity and the total solid protease sample of the crude enzyme of Pseudomonas aeruginosa and Bacillus subtilis were 0.299 U/ mL and 0.289 U/ mL, 1.37±0.14 U/mg, and 1.199 U/mg respectively. The effect on dehairing, distaining, and scum removal revealed that the purified protease enzyme of PMOJ-01 and PMOJ-05 can be used in detergent and leather industries.

Cytotoxic Effect of Pseudomonas aurogenosa Protease on Cancer Cells

2019 ◽  
Vol 10 (03) ◽  
Author(s):  
Ghanyia J. Shanyoor ◽  
Fatima R. Abdul ◽  
Nehad A. Taher ◽  
Ihsan A. Raheem
Keyword(s):  
Cell Line ◽  
Normal Cell ◽  
Cytotoxic Effect ◽  
Human Cancer ◽  
Skim Milk ◽  
Exchange Chromatography ◽  
Protease Production ◽  
Normal Cell Line ◽  
Protease Enzyme ◽  
Embryonic Fibroblast

About (20) Pseudomonas rogenosa isolate were experienced for their ability of protease production by calculating the diameter of lysis area after developing on skim milk agar medium (qualitatively ) and the results exhibited that only isolate no (5), was higher isolate for protease making of (26mm) of lysis area. Then, the protein concentration also identified by Bradford method and it was found of 0.16 mg/ ml , then purification was done by using an ion- exchange chromatography with DEAE sephadex G- 100 column and the results showed the presence of 1 peak of enzyme with 50 Kd of molecular weight 2 peaks of other proteins . we tried to investigate the invitro Cytotoxic effect of purified enzyme against two human cancer lines, HeP2 (Human larynx epidermed carcinoma ) , RD ( Rabdo- Sarcoma ) , and one normal cell line Ref ( Rat embryonic fibroblast ) . The cancer and normal cells were treated with different concentrations of protease enzyme ranging from ( 0.05, 0.1, 0.2, 0.4,0.8and 0.16 mg/ml) then incubated for additional 48h at 37C0 and the results showed highest toxicity ( 80.28%) of protease enzyme on RD , moderate cytotoxicity (45.52%) on Hep andslight toxicity ( 37.12% ) on normal cell line (Ref) in a concentration (0.8mg/ml).

Enzyme-assisted Extraction for Optimized Recovery of Phenolic Bioactives from Peganum hermala Leaves Using Response Surface Methodology

2018 ◽  
Vol 17 (4) ◽  
pp. 349-354
Author(s):  
Qadir Rahman ◽  
Anwar Farooq ◽  
Amjad Gilani Mazhar ◽  
Nadeem Yaqoob Muhammad ◽  
Ahmad Mukhtar
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Enzyme Concentration ◽  
Coumaric Acid ◽  
Assisted Extraction ◽  
Pre Treatment ◽  
Optimized Conditions ◽  
Enzyme Complexes ◽  
Hydrolysis Of ◽  
Central Composite

This study investigates the effect of enzyme formulations (Zympex-014, Kemzyme dry-plus and Natuzyme) on recovery of phenolics from Peganum hermala (harmal) leaves, under optimized conditions using response surface methodology. As compared to the other enzyme complexes, the yield (34 g/100g) obtained through Zympex-014-assisted extraction was higher under optimized conditions such as time (75 min), temperature (70°C), pH (6.5) and enzyme concentration (5 g/100 g) using central composite design (CCD). Effectiveness of Zympex-014 towards hydrolysis of P. hermala leaves cell wall was examined by analyzing the control and enzyme-treated leave residues using scanning electron microscope (SEM). GC/MS characterization authenticated the presence of quercetin (1.44), gallic acid (0.23), caffeic acid (0.04), cinnamic acid (0.05), m-coumaric acid (0.23) and p-coumaric acid (0.37 μg/g) as the potent phenolics in Zympex-014 based extract. It can be concluded from the findings of the current work that pre-treatment of P. hermala leaves with Zympex-014 significantly enhanced the recovery of phenolics that supports its potential uses in the nutra-pharamaceutical industry.

Constraints in Adoption ofModern Farm Machines by Tribal Farmers in Ramgarh District of Jharkhand

2019 ◽  
Vol 6 (03) ◽  
Author(s):  
PK SUNDARAM ◽  
BIKASH SARKAR ◽  
UJJWAL KUMAR ◽  
AP ANURAG ◽  
DK RAGHAV ◽  
...  
Keyword(s):  
Cell Line ◽  
Normal Cell ◽  
Human Cancer ◽  
Skim Milk ◽  
Exchange Chromatography ◽  
Protease Production ◽  
Normal Cell Line ◽  
Protease Enzyme ◽  
Tribal Farmers ◽  
Embryonic Fibroblast

About (20) Pseudomonas rogenosa isolate were experienced for their ability of protease production by calculating the diameter of lysis area after developing on skim milk agar medium (qualitatively ) andamp; the results exhibited that only isolate no (5), was higher isolate for protease making of (26mm) of lysis area. Then, the protein concentration also identified by Bradford method andamp; it was found of 0.16 mg/ ml , then purification was done by using an ion- exchange chromatography with DEAE sephadex G- 100 column andamp; the results showed the presence of 1 peak of enzyme with 50 Kd of molecular weight 2 peaks of other proteins . we tried to investigate the invitro Cytotoxic effect of purified enzyme against two human cancer lines, HeP2 (Human larynx epidermed carcinoma ) , RD ( Rabdo- Sarcoma ) , andamp; one normal cell line Ref ( Rat embryonic fibroblast ). The cancer andamp; normal cells were treated with different concentrations of protease enzyme ranging from ( 0.05, 0.1, 0.2, 0.4,0.8andamp; 0.16 mg/ml) then incubated for additional 48h at 37C 0 andamp; the results showed highest toxicity ( 80.28%) of protease enzyme on RD , moderate cytotoxicity (45.52%) on Hep andamp;slight toxicity ( 37.12% )on normal cell line (Ref) in a concentration (0.8mg/ml).

scholarly journals GES-2, a Class A β-Lactamase fromPseudomonas aeruginosa with Increased Hydrolysis of Imipenem

2001 ◽  
Vol 45 (9) ◽  
pp. 2598-2603 ◽  
Author(s):  
Laurent Poirel ◽  
Gerhard F. Weldhagen ◽  
Thierry Naas ◽  
Christophe De Champs ◽  
Michael G. Dove ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Amino Acid Change ◽  
Blood Cultures ◽  
Class A ◽  
Omega Loop ◽  
Cephalosporin Resistance ◽  
Lactamase Gene ◽  
Hydrolysis Of

ABSTRACT Pseudomonas aeruginosa GW-1 was isolated in 2000 in South Africa from blood cultures of a 38-year-old female who developed nosocomial pneumonia. This isolate harbored a self-transferable ca. 100-kb plasmid that conferred an expanded-spectrum cephalosporin resistance profile associated with an intermediate susceptibility to imipenem. A β-lactamase gene, bla GES-2, was cloned from whole-cell DNA of P. aeruginosa GW-1 and expressed in Escherichia coli. GES-2, with a pI value of 5.8, hydrolyzed expanded-spectrum cephalosporins, and its substrate profile was extended to include imipenem compared to that of GES-1, identified previously in Klebsiella pneumoniae. GES-2 activity was less inhibited by clavulanic acid, tazobactam and imipenem than GES-1. The GES-2 amino acid sequence differs from that of GES-1 by a glycine-to-asparagine substitution in position 170 located in the omega loop of Ambler class A enzymes. This amino acid change may explain the extension of the substrate profile of the plasmid-encoded β-lactamase GES-2.

Enhancing enzymatic hydrolysis of coconut husk through Pseudomonas aeruginosa AP 029/GLVIIA rhamnolipid preparation

2017 ◽  
Vol 237 ◽  
pp. 20-26 ◽  
Author(s):  
Cynthia Kérzia Costa de Araújo ◽  
Alan de Oliveira Campos ◽  
Carlos Eduardo de Araújo Padilha ◽  
Francisco Canindé de Sousa Júnior ◽  
Ruthinéia Jéssica Alves do Nascimento ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Enzymatic Hydrolysis ◽  
Coconut Husk ◽  
Hydrolysis Of

scholarly journals Kinetics of Enzymatic Hydrolysis of Southeast Sulawesi Sago Starch

2020 ◽  
pp. 53-61
Author(s):  
Ansharullah Ansharullah ◽  
Muhammad Natsir
Keyword(s):  
Enzymatic Hydrolysis ◽  
Maximum Velocity ◽  
Enzyme Concentration ◽  
Hydrolysis Rate ◽  
Sago Starch ◽  
Optimum Conditions ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Substrate Concentrations ◽  
Menten Constant

The aims of this study were to characterize the kinetics of enzymatic hydrolysis of sago starch, obtained from Southeast Sulawesi Indonesia. The enzyme used for hydrolysis was bacterial ∝-amylase (Termamyl 120L from Bacillus licheniformis, E. C. 3.2.1.1).  The method to determine the initial velocity (Vo) of the hydrolysis was developed by differentiation a nonlinear equation (NLE).  The Vo of the hydrolysis was measured at various pH (6.0, 6.5,and 7.0), temperatures (40, 60, 75 and 95oC), enzyme concentrations (0.5, 1.0, 1.5 and 2.0 µg per mL) and in the presence of 70 ppm Ca++. The optimum conditions of this experiment were found to be at pH 6.5 – 7.0 and 75oC, and the Vo increased with increasing enzyme concentration. The Vo values at various substrate concentrations were also determined, which were then used to calculate the enzymes kinetics constant of the hydrolysis, including Michaelis-Menten constant (Km) and maximum velocity (Vmax) using a Hanes plot.  Km and Vmax values were found to be higher in the measurement at pH 7.0 and 75oC. The Km values  at four  different combinations of pH and temperatures (pH 6.5, 40oC; pH 6.5, 75oC; pH 7.0, 40oC; pH 7.0, 75oC) were found to be 0.86, 3.23, 0.77 and 3.83 mg/mL, respectively; and Vmax values were 17.5, 54.3, 20.3 and 57.1 µg/mL/min, respectively. The results obtained showed that hydrolysis rate of this starch was somewhat low.

Sign in / Sign up

Export Citation Format

Share Document