Proteolytic enzymes produced in liquid media by Fusiformis nodosus

1964 ◽  
Vol 15 (3) ◽  
pp. 417 ◽  
Author(s):  
JH Thomas
Keyword(s):  
Enzyme Activity ◽  
Stationary Phase ◽  
Proteolytic Enzymes ◽  
Logarithmic Phase ◽  
Liquid Media ◽  
Enzyme Preparations ◽  
Stages Of Growth ◽  
Optimum Ph ◽  
Digestive Activity ◽  
Sulphydryl Compounds

Four strains of Fusiformis nodosus examined were shown to produce proteolytic enzymes digesting azocasein. When enzyme activity was plotted against the age of culture, the curves obtained showed two maxima, the first coinciding with the end of the logarithmic phase of growth, and the second with the end of the stationary phase. Enzyme preparations obtained at either of these stages of growth had similar properties, and digested casein and haemoglobin. The addition of sulphydryl compounds was without effect on the casein-digestive activity of either preparation, but enhanced the digestion of haemoglobin. The optimum pH for casein digestion by either preparation was about 9.5. Both preparations had similar stability to treatment by acid or alkali and both were inactivated by exposure to temperatures greater than 50°C.

Impact of gastric pH on dietary enzyme activity and survivability in swine fed β-glucanase supplemented diets

1996 ◽  
Vol 76 (2) ◽  
pp. 245-252 ◽  
Author(s):  
T. C. Baas ◽  
P. A. Thacker
Keyword(s):  
Enzyme Activity ◽  
Latin Square ◽  
Gastric Ph ◽  
Glucanase Activity ◽  
Enzyme Preparations ◽  
Optimum Ph ◽  
Deterioration Effect ◽  
Series Of Experiments ◽  
Ph Level ◽  
Daily Gain

A series of experiments was conducted to determine the effect of pH on β-glucanase activity and to monitor the effect of passage through the stomach on the ability of enzymes to degrade β-glucans. In exp. 1, β-glucanase activity was determined in 10 commercially available enzyme products at 5 pH levels (2.5, 3.5, 4.5, 5.5 and 6.5) using a discontinuous assay. Little activity was evident at pH 2.5, and activity was only slightly increased at pH 3.5. The highest activity occurred at pH 4.5 and 5.5. Enzyme activity declined quickly at pH 6.5. Experiment 2 evaluated the capability of β-glucanase to recover activity after incubation at suboptimal pH levels. Five enzyme preparations were incubated at three pH levels (2.5, 3.5 and 4.5) for 15, 30, 60 or 120-min. The pH level was then increased to pH 5.5, which was the optimum pH for activity determined in exp. 1. All enzyme products were relatively stable at pH 4.5 and 5.5. Enzyme products treated at pH 3.5 started to lose activity and all enzyme products exhibited a deterioration effect when incubated at pH 2.5. However, all enzymes recovered some activity upon return to pH 5.5. Experiment 3 was designed to evaluate the amount of β-glucanase activity leaving the stomach of the pig. Six barrows cannulated with a simple T-cannulae located at the start of the duodenum were used in a 6 × 6 Latin square design experiment. The diets consisted of a control and five diets supplemented with the same enzymes used in exp. 2. The level of β-glucanase activity in the digesta from pigs fed any of the diets decreased over time as pH decreased. However, across all products, 52 and 26% of initial activity could still be detected 60 and 240 min after feeding. Experiment 4 was conducted to evaluate the effectiveness of the five enzyme sources in improving the performance of pigs fed hulless barley-based diets. Supplementation of hog growing-finishing rations with any of the enzyme products failed to significantly (P > 0.05) improve daily gain, feed intake or feed efficiency. The digestibility coefficients for dry matter, crude protein and energy showed a general trend towards improved digestibility with enzyme supplementation (P > 0.05) with Biofeed producing a significant increase. The overall results of these experiments indicate that although the low pH found in the stomach of the pig is detrimental to enzyme activity, some enzyme activity is retained in the small intestine of the pig. Therefore, the low gastric pH of the pig and its effects on enzyme activity cannot completely explain the lack of response of pigs to β-glucanase. Key words: β-glucanase, pH, pig, enzyme

scholarly journals KOMPONEN METABOLIT SEKUNDER DAN AKTIVITAS ANTIOKSIDAN Spirulina fusiformis YANG DIKULTUR PADA MEDIA CAMPURAN (PUPUK R1, UREA DAN KATALIS)

2018 ◽  
Vol 5 (2) ◽  
pp. 161
Author(s):  
Nabila Ukhty
Keyword(s):  
Growth Rate ◽  
Antioxidant Activity ◽  
Stationary Phase ◽  
Secondary Metabolite ◽  
Mixed Media ◽  
Logarithmic Phase ◽  
Stages Of Growth ◽  
Death Phase ◽  
Microalgae Growth

Spirulina fusiformis is one of blue algae which can produce phycocyanin pigments. In this study used a mixed media consists of fertilizer R1, urea and catalyst as a medium for microalgae growth. This study aims to determine the growth rate, secondary metabolite component and antioxidant activity of S. fusiformis which was cultivated in a mixture media cnsists of fetilizer R1, urea and catalysts. S. fusiformis was cultured for 21 days. Based on the results of the study, it is known that S. fusiformis culture experienced five stages of growth. The logarithmic phase occurs on the 3rd day until the 10th day, the stationary phase occurs on the 10th day to the 15th day, and the death phase occurs on the 20th day. S. fusiformis biomass harvested on the 12th day contained alkaloids, flavonoids, saponins and steroids. The biomass antioxidant activity of S. fusiformis harvested on the 12th day had IC50 tilapia of 1937.41 ppm.

scholarly journals Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

Effect of temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37

2021 ◽  
Vol 66 (1) ◽  
pp. 72-79
Author(s):  
Thuoc Doan Van ◽  
Hung Nguyen Phuc
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Animal Feed ◽  
Culture Conditions ◽  
Effect Of Temperature ◽  
Physical Parameters ◽  
Original Activity ◽  
Optimum Ph ◽  
Production Activity ◽  
Ph Range

The effect of physical parameters such as temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37 was investigated. The results indicated that the optimum culture conditions for enzyme activity were pH 7.0 and 35 oC. The optimum pH and temperature for enzyme activity were 6.0 and 70 oC. The crude enzyme was found to be stable in the pH range of 5.0 to 7.0. The enzyme was stable for 1 h at a temperature from 30 to 80 oC; nearly 100% of enzyme activity remained at temperatures of 30 - 40 oC, and about 34% of original activity remained at a temperature of 80 oC. These features demonstrated that α-amylase from B. subtilis V37 can be applied in many areas such as the food, fermentation, and animal feed industries.

β-GLUCURONIDASE OF RABBIT POLYMORPHONUCLEAR LEUCOCYTES

1950 ◽  
Vol 28e (3) ◽  
pp. 69-79 ◽  
Author(s):  
R. J. Rossiter ◽  
Esther Wong
Keyword(s):  
Enzyme Activity ◽  
Blood Plasma ◽  
Substrate Concentration ◽  
Final Concentration ◽  
White Cell ◽  
Polymorphonuclear Leucocytes ◽  
Michaelis Constant ◽  
Glucuronidase Activity ◽  
Arsanilic Acid ◽  
Optimum Ph

Rabbit polymorphonuclear leucocytes contain an enzyme capable of hydrolyzing biosynthetic phenolphthalein mono-β-glucuronide. The concentration of the enzyme in the white cell is some 2000 times the concentration of the enzyme in the blood plasma. Under the conditions of study, the β-glucuronidase activity was proportional to the concentration of the enzyme. The effect of substrate concentration on the enzyme activity was studied and the Michaelis constant, Ks, determined. The course of the reaction was linear with time for the first 12 hr. and then fell off slightly during the next 12 hr. The optimum pH of the enzyme was 4.45 in either 0.2 M acetate or 0.2 M phthalate buffer. It was not inhibited by cyanide, azide, iodoacetate, fluoride, glycine, thiourea, urethane, arsanilic acid, acetophenone, o-cresol or m-cresol, in a final concentration of 0.01 M. The possible function of β-glucuronidase in rabbit polymorphonuclear leucocytes is discussed.

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

scholarly journals Lignolytic Enzyme Activity of Isolated Bacteria from Termite (Coptotermes Sp.) and Milkfish (Chanos chanos Forsskal, 1775) Guts

2021 ◽  
Vol 13 (1) ◽  
pp. 70-76
Author(s):  
Emi Latifah ◽  
Putri Dwi Mulyani ◽  
Yekti Asih Purwestri
Keyword(s):  
Enzyme Activity ◽  
Bacillus Licheniformis ◽  
Test Method ◽  
Chanos Chanos ◽  
Enzyme Isolation ◽  
Optimum Ph ◽  
Qualitative Test ◽  
Pseudomonas Alcaligenes ◽  
Enzyme Source ◽  
Brevibacillus Parabrevis

Bacteria BSR 2, Pseudomonas alcaligenes (BSR 3), Brevibacillus parabrevis (BSR 8), Brevibacillus sp. (BSR 9), isolated from termite gut and Bacillus licheniformis (BSA B1) isolated from milkfish gut have been known to possess celluloytic activity. However, their lignolytic ability has not been known. This study aimed to determine the lignolytic ability of bacteria isolated from termit (Coptotermes sp.) and milkfish (Chanos chanos Forsskal, 1775) guts and their enzymes characterization. The qualitative test was done through the spot test method, while quantitative assay was performed spectrophotometrically at 335 nm to calculate vanillin concentration. The isolates were grown in Lignin Mineral Medium, then the optical density (OD620) were measured every 24 hours for 5 days using spectrophotometer to determine their growth profile and the best isolation time of the lignolytic enzyme. Based on results, the best lignolytic enzyme isolation time for strains Bacillus licheniformis (BSA B1) and BSR 2 were 5 days, yielding lignolytic enzyme activity of 0.961 ± 0.168 U/mg and 2.176 ± 0.088 U/mg respectively,  while strains Pseudomonas alcaligenes (BSR 3), Brevibacillus parabrevis (BSR 8), and Brevibacillus sp. (BSR 9) were 4 days, yielding of 1.206 ± 0.045 U/mg, 1.162 ± 0.191 U/mg, and 0.896 ± 0.108 U/mg, respectively. The strain BSR 2 showed the highest lignolytic activity compared to other strains. The optimum temperature for lignolytic enzyme activity of BSR 2 was 30 ℃ and the optimum pH was 7. The lignolytic enzyme activity showed that these bacterial isolates can be a chance to be used as new alternative lignolytic enzyme source in commercial bioconversion process.

scholarly journals Pre-fermentative treatment of a model wine with aim to serve as a functional food with decreased alcohol content

2017 ◽  
Vol 63 (01) ◽  
pp. 47-53
Author(s):  
Irina Mladenoska ◽  
Verica Petkova ◽  
Tatjana Kadifkova Panovska
Keyword(s):  
Enzyme Activity ◽  
Gluconic Acid ◽  
Functional Food ◽  
Ph Value ◽  
Enzymatic Reaction ◽  
Alginate Beads ◽  
High Concentration ◽  
Ph Optimum ◽  
Enzyme Preparations ◽  
Initial Ph

The effect of substrate concentration on the enzyme activity in the reaction of glucose conversion into gluconic acid was investigated by using three different enzyme preparations in media with two different glucose concentrations. The media were simulating the conditions in the must, thus named as minimal model must, and were composed form combination of several organic acids and glucose. Those media were having initial pH of 3.5 that is a very unfavorable for glucose oxidase activity having a pH optimum at the pH value of 5.5. Among the three preparations used, the bakery additive, Alphamalt Gloxy 5080, was the most active in the medium with glucose concentration of 10 g/L, showing conversion of more than 70% for the period of 24 h, while the same enzyme preparation in the medium with 100 g/L glucose converted only about 7% of glucose. The pH value of the medium at the beginning and at the end of the enzymatic reaction was a good indicator of the enzyme activity. It seems that for the conversion of glucose in higher concentration, enzymatic preparation in high concentration should also be used. The preliminary attempt of immobilization of two preparations of glucose oxidases in alginate beads was also performed and a successful immobilization procedure for utilization in food industry was preliminarily developed. Keywords: glucose oxidases, enzymatic pretreatment, glucose, gluconic acid, model wine, functional food

scholarly journals Induction of the synthesis of an additional family of long-chain dolichols in the yeast Saccharomyces cerevisiae. Effect of starvation and ageing.

2002 ◽  
Vol 49 (3) ◽  
pp. 781-787 ◽  
Author(s):  
Anna Szkopinska ◽  
Ewa Swiezewska ◽  
Joanna Rytka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stationary Phase ◽  
Yeast Cells ◽  
Logarithmic Phase ◽  
Cellular Membranes ◽  
Yeast Saccharomyces Cerevisiae ◽  
Chemical Changes ◽  
Physico Chemical ◽  
Long Chain

The yeast Saccharomyces cerevisiae strain W303 synthesizes in the early logarithmic phase of growth dolichols of 14-18 isoprene residues. The analysis of the polyisoprenoids present in the stationary phase revealed an additional family which proved to be also dolichols but of 19-24 isoprene residues, constituting 39% of the total dolichols. The transfer of early logarithmic phase cells to a starvation medium lacking glucose or nitrogen resulted in the synthesis of the longer chain dolichols. The additional family of dolichols represented 13.8% and 10.3% of total dolichols in the glucose and nitrogen deficient media, respectively. The level of dolichols in yeast cells increased with the age of the cultures. Since both families of dolichols are present in stationary phase cells we postulate that the longer chain dolichols may be responsible for the physico-chemical changes in cellular membranes allowing yeast cells to adapt to nutrient deficient conditions to maintain long-term viability.

Effects of pretreatments with sulfhydryls and alkylating agents on spheroplast formation from Schwanniomyces species

1984 ◽  
Vol 30 (3) ◽  
pp. 368-374 ◽  
Author(s):  
T. M. Dowhanick ◽  
C. J. Panchal ◽  
G. G. Stewart
Keyword(s):  
Cell Wall ◽  
Stationary Phase ◽  
Growth Phase ◽  
Cell Walls ◽  
Alkylating Agents ◽  
Inhibitory Effects ◽  
Late Stationary Phase ◽  
Stages Of Growth ◽  
Degradative Enzymes ◽  
Sulfhydryl Compounds

Pretreatment of cells with β-mercaptoethanol, dithiothreitol, or cysteine increased the rate of spheroplast formation at all stages of growth in Schwanniomyces castellii and S. occidentalis, but had little effect on final yields of spheroplasts when compared with controls. Pretreatment with iodoacetate and cystine resulted in decreased rates of formation and lower yields of spheroplasts at all stages of growth for both species. The enhanced rates of spheroplast formation in the presence of the sulfhydryl compounds were more pronounced when the experimental cells were derived from early or late stationary phase cultures, whereas the inhibitory effects of cystine and iodoacetate were not associated with the growth phase. In agreement with extant data on other yeast genera, sulfhydryl compounds increased the susceptibility of the yeast cell wall to degradative enzymes, whilst alkylating agents decreased susceptibility of cell walls to these enzymes.

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