Hydrolysis of Phosphates by Enzyme Preparations Derived from Carious Dentine, Bacterial Plaque and Saliva

1970 ◽  
Vol 4 (1) ◽  
pp. 14-22 ◽  
Author(s):  
K.K. Mäkinen
Keyword(s):  
Enzyme Preparations ◽  
Carious Dentine ◽  
Bacterial Plaque ◽  
Hydrolysis Of

SOME ASPECTS OF THE ENZYMIC HYDROLYSIS OF URINARY 17-KETOSTEROID CONJUGATES

1960 ◽  
Vol 38 (1) ◽  
pp. 769-776
Author(s):  
R. Hobkirk ◽  
J. J. Cohen
Keyword(s):  
Liver Enzymes ◽  
Striking Difference ◽  
Degree Of Hydrolysis ◽  
Enzyme Preparations ◽  
Bacterial Preparation ◽  
Bacterial Enzyme ◽  
The Difference ◽  
Normal Urine ◽  
High Degree ◽  
Hydrolysis Of

Four enzyme preparations containing β-glucuronidase, of bacterial, mammalian, and molluscan origin, have been shown to be equally effective in liberating 17-ketosteroids (17-KS) of the 5β-(etiocholane) configuration in normal urine. The bacterial preparation releases steroids of the 5α-(androstane) configuration more rapidly than do the molluscan enzymes and with much greater ease than does the liver enzyme. In view of the data obtained it seems unlikely that the striking difference between the bacterial and liver enzymes can be due to the hydrolysis of some labile conjugate, such as sulphate, by the former and not by the latter. Possibilities that the difference is due to the hydrolysis of an unknown type of urinary conjugate by the bacterial preparation, or to the low specificity of the bacterial β-glucuronidase, are discussed. The high degree of hydrolysis of 17-KS conjugates by the bacterial enzyme followed by solvolysis suggests this as a most useful hydrolytic procedure.

SOME ASPECTS OF THE ENZYMIC HYDROLYSIS OF URINARY 17-KETOSTEROID CONJUGATES

1960 ◽  
Vol 38 (7) ◽  
pp. 769-776 ◽  
Author(s):  
R. Hobkirk ◽  
J. J. Cohen
Keyword(s):  
Liver Enzymes ◽  
Striking Difference ◽  
Degree Of Hydrolysis ◽  
Enzyme Preparations ◽  
Bacterial Preparation ◽  
Bacterial Enzyme ◽  
The Difference ◽  
Normal Urine ◽  
High Degree ◽  
Hydrolysis Of

Four enzyme preparations containing β-glucuronidase, of bacterial, mammalian, and molluscan origin, have been shown to be equally effective in liberating 17-ketosteroids (17-KS) of the 5β-(etiocholane) configuration in normal urine. The bacterial preparation releases steroids of the 5α-(androstane) configuration more rapidly than do the molluscan enzymes and with much greater ease than does the liver enzyme. In view of the data obtained it seems unlikely that the striking difference between the bacterial and liver enzymes can be due to the hydrolysis of some labile conjugate, such as sulphate, by the former and not by the latter. Possibilities that the difference is due to the hydrolysis of an unknown type of urinary conjugate by the bacterial preparation, or to the low specificity of the bacterial β-glucuronidase, are discussed. The high degree of hydrolysis of 17-KS conjugates by the bacterial enzyme followed by solvolysis suggests this as a most useful hydrolytic procedure.

Blending of cellulolytic enzyme preparations from different fungal sources for improved cellulose hydrolysis by increasing synergism

RSC Advances ◽  
2014 ◽  
Vol 4 (84) ◽  
pp. 44726-44732 ◽  
Author(s):  
Mukund Adsul ◽  
Bhawna Sharma ◽  
Reeta Rani Singhania ◽  
Jitendra Kumar Saini ◽  
Ankita Sharma ◽  
...  
Keyword(s):  
Wheat Straw ◽  
Cellulose Hydrolysis ◽  
Cellulolytic Enzyme ◽  
Enzyme Preparations ◽  
Fungal Enzyme ◽  
Enzyme Cocktail ◽  
Different Types ◽  
Hydrolysis Of

A prepared enzyme cocktail from different fungal enzyme preparations increases the hydrolysis of avicel/wheat straw by increasing synergism between the same or different types of cellulases.

scholarly journals The hydrolysis of glycosyl fluorides by glycosidases

1967 ◽  
Vol 105 (2) ◽  
pp. 669-672 ◽  
Author(s):  
J. E. G. Barnett ◽  
W. T. S. Jarvis ◽  
K A Munday
Keyword(s):  
Helix Pomatia ◽  
Enzyme Preparations ◽  
Intestinal Juice ◽  
Hydrolysis Of ◽  
Specific Inhibitors

1. α-d- and β-d-Glucopyranosyl, α-d- and β-d-galactopyranosyl, α-d-mannopyranosyl and α-d-xylopyranosyl fluorides were hydrolysed specifically by the respective glycosidases from several sources. 2. Use of specific inhibitors with a mixture of glycosidases from Helix pomatia intestinal juice showed that each glycosyl fluoride was hydrolysed only by the respective glycosidase. α-d-Glucopyranosidase and α-d-xylopyranosidase activities were shown to be due to different enzymes. 3. Partially purified enzyme preparations containing only one of the glycosidase activities hydrolysed only the corresponding glycosyl fluoride. 4. The configuration at C-1 of α-d-mannopyranosyl fluoride was confirmed since it was hydrolysed by an α-d-mannosidase preparation that contained no detectable β-d-mannosidase activity. 5. An attempt to prepare o-nitrophenyl β-d-mannopyranoside led only to o-nitrophenyl α-d-mannopyranoside.

scholarly journals Development of a concept for the production of wheat snacks with the elimination of gluten by the biocatalysis

2021 ◽  
Vol 82 (4) ◽  
pp. 77-83
Author(s):  
A. Y. Sharikov ◽  
E. N. Sokolova ◽  
M. V. Amelyakina ◽  
T. V. Yuraskina ◽  
V. V. Ivanov ◽  
...  
Keyword(s):  
Protein Modification ◽  
Raw Materials ◽  
Amino Acid Sequences ◽  
Practical Implementation ◽  
Specific Amino Acid ◽  
Enzyme Preparations ◽  
Molecular Weights ◽  
Enzyme Systems ◽  
Antigenic Properties ◽  
Hydrolysis Of

The increase in the number of cases of allergic reactions and celiac disease is an important problem. The solution to this problem is the search and development of relevant and effective ways to eliminate gluten. Specific amino acid sequences glutamine and proline determine the resistance to protease hydrolysis of the structural domains of gluten fractions. The analysis of the literature data showed that an alternative to the gluten-free diet is the use of biotechnological methods for modifying ingredients containing gluten. Such methods include the use of leavens on the base of lactic acid bacteria or enzyme preparations containing peptidases specific to gluten biocatalysis. In addition, the pretreatment of raw materials by extrusion cooking contributes to an increase in the degree of gluten hydrolysis. The effect of the thermoplastic extrusion and various enzyme systems containing proteases, amylolytic, cellulolytic and hemicellulolytic enzymes on the changes in the molecular weights of wheat protein fractions was studied. It was found that extrusion as a factor of protein modification significantly affects the proteolysis of wheat proteins using enzyme systems of different substrate specificity. The most effective hydrolysis was shown by the use of a complex enzyme preparation Amyloprotoorizin. including The effect was also noted after bioconversion of non-extruded wheat. An algorithm for the technology of wheat snacks based on the processes of extrusion and biocatalysis of proteins with specific proteases for the elimination of gluten is devepoped. The practical implementation of the technology will make it possible to obtain ready-to-eat snacks, which will be investigated for the preservation or elimination of antigenic properties during clinical trials.

scholarly journals HYDROLYTIC REGULATION OF COMPONENT PROPERTIES

2020 ◽  
Vol 6 (444) ◽  
pp. 23-28
Author(s):  
V. A. Asafov ◽  
◽  
N. L. Tankova ◽  
E. L. Iskakova ◽  
T. N. Golovach ◽  
...  
Keyword(s):  
Raw Materials ◽  
Farm Animals ◽  
Animal Origin ◽  
Enzyme Preparations ◽  
Global Trends ◽  
Antigenic Activity ◽  
The Republic ◽  
Protein Components ◽  
Hydrolysis Of ◽  
Plant Sources

. The article provides an assessment of the dairy farming need in the Russian Federation and the Republic of Belarus in calves feed. The main global trends aimed at providing young animals with high-quality food means are considered. Various variants of directed hydrolysis of calf milk replacer (CMR) protein components intended for feeding young animals in the first months of life are analyzed. The possibilities of reducing the soy proteins antigenic activity, which are widely used at present in the CMR formulations for feeding young farm animals, are discussed. The results of experimental work and patents are presented, which describe the most widely used approaches to the production of enzymatic hydrolysates of proteins with desired properties, as well as the assessment of their biological activity and immunochemical properties. The issues of using various enzyme preparations of bacterial, fungal and animal origin for hydrolysis of colostrum proteins and plant sources of protein raw materials for the CMR production are considered.

scholarly journals Enzymatic hydrolysis of potato starch and ethanol production

2004 ◽  
Vol 58 (7-8) ◽  
pp. 322-326 ◽  
Author(s):  
Miodrag Lazic ◽  
Suzana Raskovic ◽  
Mihajlo Stankovic ◽  
Vlada Veljkovic
Keyword(s):  
Particle Size ◽  
Enzymatic Hydrolysis ◽  
Ethanol Production ◽  
Potato Starch ◽  
Enzyme Hydrolysis ◽  
Potato Flour ◽  
Yeast Saccharomyces Cerevisiae ◽  
Enzyme Preparations ◽  
Dextrose Equivalent ◽  
Hydrolysis Of

The hydrolysis of potato starch using one (Termamyl or Fungamyl) and two combined (Termamyl and Supersan) commercial enzyme preparations and ethanol production from the hydrolysates obtained using the yeast Saccharomyces cerevisiae were studied. Potato tubers were previously prepared as mash or flour. The study dealt with the effects of the hydromodulus (1:1 and 1:0.5), particle size (0.1, 0.2 and 0.4 mm) as well as the type and concentration of enzyme on the enzymatic hydrolysis of potato starch. The highest dextrose equivalent (79.3%, DE) was achieved during two-enzyme hydrolysis (combination of two enzyme preparations: Termamyl 14.4 KNU/dm3 and Supersan 28.8 AGU/dm3) of starch from potato flour (particle size: 0.1-0.2 mm) at an inital starch concentration of 75 g/dm3. During the two-enzyme hydrolysis, a lower DE (61%) was achieved when potato mash was used as a starch source. Using Termamyl (14,4 KNU/dm3) and potato mash a higher DE was achieved at the hydromodulus 1:1 (51.2%) than at the hydromodulus 1:0.5 (40.9%). The highest ethanol concentration (5.0 vol%) was obtained when the hydrolyzate of potato flour from the two-enzyme process was used as a substrate for alcoholic fermentation.

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