scholarly journals Rice bran as a substrate for proteolytic enzyme production

2006 ◽  
Vol 49 (5) ◽  
pp. 843-851 ◽  
Author(s):  
Alagarsamy Sumantha ◽  
Paul Deepa ◽  
Chandran Sandhya ◽  
George Szakacs ◽  
Carlos Ricardo Soccol ◽  
...  
Keyword(s):  
Rice Bran ◽  
Enzyme Production ◽  
Proteolytic Enzyme ◽  
Initial Moisture Content ◽  
Fold Increase ◽  
Maximal Activity ◽  
Protease Production ◽  
Rhizopus Microsporus ◽  
Rhizopus Sp ◽  
Optimized Conditions

Rice bran was used as the substrate for screening nine strains of Rhizopus sp. for neutral protease production by solid-state fermentation. The best producer, Rhizopus microsporus NRRL 3671, was used for optimizing the process parameters for enzyme production. Fermentation carried out with 44.44 % initial moisture content at a temperature of 30 C for 72 h was found to be the optimum for enzyme secretion by the fermenting organism. While most of the carbon supplements favored enzyme production, addition of casein resulted in a marginal increase in protease yield. Fermentation was then carried out under optimized conditions to obtain the crude extract of the enzyme, which was partially purified by precipitation and dialysis. A 3-fold increase in the enzyme purity was achieved in this manner. The enzyme was found to be a metalloprotease, being activated by Mn2+, with maximal activity at a temperature of 60 C and pH 7.0.

Statistical Optimization of the production of protease from Bacillus sp. MSK-01 in submerged fermentation

2018 ◽  
Vol 23 (4) ◽  
Author(s):  
Kulwant Kaur ◽  
Sonica Sondhi ◽  
Palki Sahib Kaur
Keyword(s):  
Submerged Fermentation ◽  
Milk Powder ◽  
Skim Milk ◽  
Fold Increase ◽  
Skim Milk Powder ◽  
Protease Production ◽  
High Yield ◽  
Bacillus Sp ◽  
Increasing Demand ◽  
Optimized Conditions

Protease has been in increasing demand in industries due to its hydrolytic nature. In industries, high yield of enzyme is required to meet the industrial need at a relatively cheaper cost. In the present study, the protease from Bacillus sp. MSK-01 was produced in large quantity by submerged fermentation. Statistical techniques including Plackett-Burman and Response surface methodology are useful tools for optimizing many parameters at a time and are used for increasing the protease production from Bacillus sp. MSK-01. 19 different parameters were chosen, out of which 15 factors had positive effect on protease yield. Four maximum influencing factors were peptone, magnesium sulphate, skim milk powder and casein were chosen to further increase the protease yield. 397.3 IU ml-1 of enzyme yield was obtained under optimized conditions which lead to 198 fold increase in the yield of protease from unoptimized condition. 

scholarly journals Isolation of Thermostable Protease Producing Bacteria from the Microbial Mats

2021 ◽  
Vol 23 (10) ◽  
pp. 222-235
Author(s):  
Malathi, M ◽  
◽  
Latha, D ◽  
Keyword(s):  
Enzyme Production ◽  
Microbial Mats ◽  
Skim Milk ◽  
Inoculum Size ◽  
Protease Production ◽  
Carbon And Nitrogen ◽  
Test Culture ◽  
Higher Temperature ◽  
Optimized Conditions ◽  
Near Future

As thermostable protease has more commercial value in different industries, the aim of this study was to search for such an enzyme producing bacteria from the microbial mats. Investigation was continued on the isolate for its ability to produce mass amount of enzyme and its activity under suitable optimized conditions. Different parameters including cheap carbon and nitrogen substrates, inoculum size and temperature was selected to optimize the enzyme production conditions. Initially five different isolates from two microbial mats collected from different sources were analyzed for its ability to produce thermostable protease after exposing to higher temperature incubation conditions. Test culture tentatively named as 1F from microbial mat-1 was selected as more enzyme producer among the ten isolates. The organism was selected based on the zone of clearance on skim milk agar by the isolate, that indicating more protease production. Under each optimization parameter, each type of carbon (Lactose), and nitrogen (yeast extract) source showed more enzyme production and activity respectively. About 1% inoculum size and a thermostable temperature of 45°C produced significant amount of enzyme and its activity. The obtained results emphasized the need for thermostable protease for different commercial industries in the existing and near future.

scholarly journals Novel Application of Mahua (Madhuca sp.) Flowers for Augmented Protease Production from Aeromonas sp. S1

2012 ◽  
Vol 7 (10) ◽  
pp. 1934578X1200701 ◽  
Author(s):  
Amrik Bhattacharya ◽  
Vandana Saini ◽  
Anshu Gupta
Keyword(s):  
Enzyme Production ◽  
Low Cost ◽  
Inoculum Size ◽  
Protease Production ◽  
Agitation Rate ◽  
Value Addition ◽  
New Approach ◽  
Flower Extract ◽  
Optimized Conditions ◽  
Optimum Production

The present study explored the utilization of Mahua ( Madhuca sp.) flowers, a major non-timber forest product (NTFP) of India, as a low-cost, natural substrate for protease production under submerged fermentation. Bacterial strain Aeromonas sp. S1, previously reported by us, was used as the protease producer. Using Mahua flower extract (MFE) as the medium additive, the protease production could successfully be enhanced by 5.6-fold (564.5 UmL−1) after 24 h of fermentation under optimized conditions compared with initial production of 99.9 UmL−1 in the absence of MFE. The cultural parameters for optimum production of protease were determined to be: incubation time-24 h; pH-7.0; MFE concentration-5% (v/v); inoculum size-0.3% (v/v) and agitation rate-200 rpm. The results obtained demonstrate the potential of cheaper and abundantly available Mahua flowers for induction of proteases, and thus offer a new approach for value addition to this biomass through industrial enzyme production.

Statistical Optimization of the Production of alpha-Amylase from Bacillus licheniformis MTCC 1483 Using Paddy Straw as Substrate

2017 ◽  
Vol 23 (2) ◽  
Author(s):  
Palki Sahib Kaur ◽  
Sukhjeet Kaur ◽  
Hardish Kaur ◽  
Sonica Sondhi
Keyword(s):  
Solid State ◽  
Bacillus Licheniformis ◽  
Solid State Fermentation ◽  
Enzyme Production ◽  
Cost Effective ◽  
Fold Increase ◽  
Paddy Straw ◽  
Cost Effective Method ◽  
Increasing Demand ◽  
Optimized Conditions

?-Amylase has been in increasing demand in industries due to its hydrolytic nature. Solid state fermentation (SSF) is a cost effective method for increasing the enzyme production. In the present study, amylase from Bacillus licheniformis MTCC 1483 was produced in large quantity by solid state fermentation using paddy straw as substrate. Response surface methodology is a useful tool for optimizing many parameters at a time and is used for increasing the amylase production. 8523 IUg-1 of enzyme activity was obtained under optimized conditions which lead to 35 fold increase in the yield of amylase from unoptimized condition.

scholarly journals Gastrointestinal Mucormycosis following aStreptococcus pyogenesToxic Shock Syndrome in a Previously Healthy Patient: A Case Report

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Jean-François Roussy ◽  
Catherine Allard ◽  
Guy St-Germain ◽  
Jacques Pépin
Keyword(s):  
Case Report ◽  
Opportunistic Infection ◽  
Streptococcus Pyogenes ◽  
Toxic Shock Syndrome ◽  
Immunocompromised Patients ◽  
Healthy Patient ◽  
Toxic Shock ◽  
Rhizopus Microsporus ◽  
First Case ◽  
Rhizopus Sp

Mucormycosis is an uncommon opportunistic infection and the gastrointestinal form is the rarest.Rhizopus sp. is the most frequent pathogen and infection occurs almost exclusively in immunocompromised patients. We describe the first case of intestinal mucormycosis occurring after aStreptococcus pyogenestoxic shock syndrome in a previously healthy patient caused byRhizopus microsporusvar.azygosporus.

Bioprocess development to add value to canola cake used as substrate for proteolytic enzyme production

2015 ◽  
Vol 95 ◽  
pp. 173-182 ◽  
Author(s):  
A.C. Freitas ◽  
F.C.F. Baleeiro ◽  
R.F. Fonseca ◽  
V. Bertucci Neto ◽  
G.A.S. Pinto ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Proteolytic Enzyme ◽  
Bioprocess Development

Effect of growth conditions on the production of manganese peroxidase by three strains of Bjerkandera adusta

2001 ◽  
Vol 47 (4) ◽  
pp. 277-282 ◽  
Author(s):  
Yuxin Wang ◽  
Rafael Vazquez-Duhalt ◽  
Michael A Pickard
Keyword(s):  
Rice Bran ◽  
Manganese Peroxidase ◽  
Enzyme Production ◽  
Scale Up ◽  
Growth Conditions ◽  
White Rot ◽  
Stirred Tank ◽  
Bjerkandera Adusta ◽  
Stirred Tank Reactors ◽  
Cereal Bran

We were looking for a strain of Bjerkandera adusta that produces high titres of manganese peroxidase under optimal conditions for large-scale enzyme purification. We have chosen two strains from the University of Alberta Microfungus Collection and Herbarium, UAMH 7308 and 8258, and compared the effects of growth conditions and medium composition on enzyme production with the well-characterized strain BOS55 (ATCC 90940). Of four types of cereal bran examined, rice bran at 3% (w/v) in 60 mM phosphate buffer pH 6 supported the highest levels of enzyme production. Using 100 mL medium in 500-mL Erlenmeyer flasks, maximum enzyme levels in the culture supernatant occurred after about 10 days of growth; 5.5 U·mL–1 for UAMH 7308, 4.4 U·mL–1 for UAMH 8258, and 1.7 U·mL–1 for BOS55, where units are expressed as micromoles of Mn-malonate formed per minute. Growth as submerged cultures in 10-L stirred tank reactors produced 3.5 U·mL–1 of manganese peroxidase (MnP) by UAMH 8258 and 2.5 U·mL–1 of MnP by 7308, while enzyme production by BOS55 was not successful in stirred tank reactors but could be scaled up in 2-L shake flasks containing 400 mL rice bran or glucose – malt – yeast extract (GMY) – Mn-glycolate medium to produce MnP levels of 1.7 U·mL–1. These results show that the two strains of B. adusta, UAMH 7308 and 8258, can produce between two and three times the manganese peroxidase level of B. adusta BOS55, that they are good candidates for scale up of enzyme production, and that the rice bran medium supports higher levels of enzyme production than most previously described media.Key words: growth conditions, cereal bran, manganese peroxidase, Bjerkandera adusta, white rot fungi.

Differential regulation of mRNAs encoding for rat intestinal alkaline phosphatase

1990 ◽  
Vol 259 (1) ◽  
pp. G93-G98 ◽  
Author(s):  
R. Eliakim ◽  
S. Seetharam ◽  
C. C. Tietze ◽  
D. H. Alpers
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Cdna Probe ◽  
Fold Increase ◽  
Maximal Activity ◽  
Amino Acid Residues ◽  
Intestinal Alkaline Phosphatase ◽  
Mrna Accumulation ◽  
Dihydroxyvitamin D3 ◽  
Fat Feeding

A cDNA probe encoding the entire structural region of the 62-kDa rat intestinal alkaline phosphatase from amino acid residues 1 to 531 detected multiple mRNA species (3.0, 2.7, and 2.2 kb) in rat intestinal RNA. The 3.0-kb species was most evident in duodenum but could be easily detected in jejunum using a 48-mer oligonucleotide encoding amino acid residues 492-508. This 48-mer oligonucleotide bound preferentially to the 3.0-kb mRNA, suggesting that the 2.7-kb mRNA differed in this region. To determine whether each of the mRNAs encoding rat intestinal alkaline phosphatase responded coordinately to physiological stimuli, the full-length cDNA and the 48-mer oligonucleotide were used as probes for the 2.7- and 2.2-kb and the 3.0-kb mRNAs, respectively. Intestinal mRNA concentration was measured by Northern blot analysis in acute (single feed, 17 kcal) and chronic (3 wk, 30% fat diet) fat feeding and in rachitic rats after 1,25-dihydroxyvitamin D3 therapy. There was a large increase (8- to 25-fold) in the 3.0-kb mRNA 7 h after acute fat feeding, with a much smaller increase (1.4- to 5.0-fold) in the 2.7- and 2.2-kb species. The peak in 3.0-kb mRNA accumulation correlated in time with the maximal activity of serum phosphatase activity after acute fat feeding (4- to 5-fold increase). In contrast, there was a much smaller increase in all mRNAs and in tissue and serum enzyme activity after chronic fat feeding.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN

1945 ◽  
Vol 81 (6) ◽  
pp. 573-592 ◽  
Author(s):  
Stuart D. Elliott
Keyword(s):  
Proteolytic Enzyme ◽  
Potassium Cyanide ◽  
Maximal Activity ◽  
Serial Passage ◽  
Iodoacetic Acid ◽  
Broth Culture ◽  
Mouse Serum ◽  
Group A Streptococci ◽  
Extracellular Proteolytic Enzyme ◽  
Group A

1. Group A streptococci sometimes produce in broth culture an extracellular proteolytic enzyme. 2. Under suitable cultural conditions the enzyme has been demonstrated in representative cultures of most of the Griffith types. Its production by a given strain may be suppressed by serial passage through mice and the variant so produced has been found to maintain this change in character on subculture in artificial media. 3. Under certain conditions, the enzyme attacks the type-specific M antigens of all the group A streptococci so far tested, with the exception of that of type 28. The enzyme exhibits its maximal activity at 37°C.: Extracts made from enzyme-producing cultures which have been grown at this temperature lack the M antigen; enzyme-producing strains may sometimes be induced to yield M substance in extracts by culturing the streptococci at 22° C. Cultures which, when grown at 37° C. yield M substance in extracts, do not produce the enzyme. 4. Human and rabbit fibrin are attacked and streptococcal fibrinolysin is also inactivated by the enzyme. Other susceptible substrates include casein, milk, gelatin, and benzoyl-l-arginineamide but not l-leucylglycylglycine. 5. The general properties of the enzyme resemble those of papain and some of the cathepsins: It is active under the reducing conditions produced in broth cultures by the presence of living bacteria; it is also activated by substances which reduce disulfide to sulfhydryl groups, e.g. potassium cyanide, cysteine, glutathione, and thioglycollic acid, but it is not activated by ascorbic acid. The enzyme is inactivated by iodoacetic acid and also by normal rabbit or mouse serum.

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