Production of amylases by yeasts

1990 ◽  
Vol 36 (11) ◽  
pp. 751-753 ◽  
Author(s):  
Valter R. Linardi ◽  
Katia M. G. Machado
Keyword(s):  
Enzymatic Activity ◽  
Key Words ◽  
Wheat Bran ◽  
Aureobasidium Pullulans ◽  
Natural Habitats ◽  
Semisolid Medium ◽  
Debranching Enzyme ◽  
Candida Kefyr ◽  
Candida Famata ◽  
High Enzymatic Activity

Yeasts (228) isolated for natural habitats were screened for their ability to produce amylases in semisolid medium of wheat bran. Strains of Aureobasidium pullulans, Candida famata, and Candida kefyr showed high enzymatic activity for α-amylase, glucoamylase, and debranching enzyme. Key words: Aureobasidium, Candida, amylolytic yeasts, α-amylase, glucoamylase.

Enzymatic activity of yeasts isolated from the inflamed mammary secretion in dairy cows

2011 ◽  
Vol 14 (1) ◽  
pp. 65-68 ◽  
Author(s):  
W. Wawron ◽  
M. Bochniarz ◽  
M. Szczubiał
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Dairy Cows ◽  
Hydrolytic Enzymes ◽  
Candida Krusei ◽  
Individual Species ◽  
Candida Kefyr ◽  
Candida Famata ◽  
Candida Lusitaniae ◽  
Leucine Arylamidase

Enzymatic activity of yeasts isolated from the inflamed mammary secretion in dairy cows The aim of the study was to evaluate enzymatic activities of yeasts isolated from inflammatory mammary secretion. The yeasts isolated from cows with clinical and sub-clinical mastitis (134 strains) included: Candida krusei (62 strains), Candida kefyr (48 strains), Candida lusitaniae (17 strains) and Candida famata (7 strains). The API ZYM system was used containing substrates to assess 19 hydrolytic enzymes. Substantial differences in the number and activity of hydrolyses were demonstrated in individual species. In Candida krusei, acid phosphatase showed the highest activity (4.36 points), in Candida kefyr and Candida lusitaniae - leucine arylamidase (4.93 and 4.25 points, respectively), in Candida famata - α-glucosidase (4.75 points). No activity of trypsin, chymotrypsin, α-galactosidase, β-glucuronidase, α-mannosidase or α-fucosidase was observed in any of the yeasts examined.

Organic−Inorganic Hybrid Silica Monolith Based Immobilized Trypsin Reactor with High Enzymatic Activity

2008 ◽  
Vol 80 (8) ◽  
pp. 2949-2956 ◽  
Author(s):  
Junfeng Ma ◽  
Zhen Liang ◽  
Xiaoqiang Qiao ◽  
Qiliang Deng ◽  
Dingyin Tao ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Inorganic Hybrid ◽  
Silica Monolith ◽  
Hybrid Silica ◽  
Immobilized Trypsin ◽  
High Enzymatic Activity

scholarly journals Efficacy of Liquid Protein Hydrolysate from Chicken Feather by Pseudomonas sp. on the Growth of Cucumis sativus

2020 ◽  
Vol 2 (1) ◽  
pp. 16
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Activity ◽  
Cucumis Sativus ◽  
Protein Hydrolysate ◽  
Antibacterial Properties ◽  
Full Potential ◽  
Pseudomonas Sp ◽  
Chicken Feather ◽  
Chicken Feathers ◽  
High Enzymatic Activity

Keratin, which made up the chicken feather, is difficult to be broken down by the proteolytic enzyme. Annually, millions of tons of chicken feathers are disposed of worldwide as waste without realizing the high protein content in the feather. Due to the presence of keratinase from keratinolytic bacteria, chicken feathers are disposed of together with poultry excreta. Therefore, this study is conducted to study the ability of liquid protein hydrolysate produced by bacteria in poultry excreta to utilize into biofertilizing and biocontrol. Keratinolytic bacteria are identified from poultry excreta by screening. The isolated enzyme was optimized in various conditions such as different pH, temperature, and feather concentration as well as nitrogen and carbon sources. Enzymatic activity increased gradually from 1% to 5% in carbon and nitrogen sources. Liquid protein hydrolysate was used to study the biofertilizing ability on the growth of Cucumis sativus and antibacterial effect on Escherichia coli. Pseudomonas sp. has the capability to degrade the feather on 10th day due to the high enzymatic activity. Pseudomonas sp. shows high enzymatic activity at 37⁰C, pH 8, and feather concentration at 0.5%. The chlorophyll estimation shows a p-value<0.05 after being treated with liquid protein hydrolysate. Liquid protein hydrolysate promoted the growth of Cucumis sativus as well as Pseudomonas sp. The antibacterial properties can also be seen against Escherichia coli. In a nutshell, chicken feather produces liquid protein hydrolysate, which has biofertilizing properties. The full potential of liquid hydrolysate can be understood with further analysis of peptide in protein hydrolysate.

Pikeperch (Stizostedion lucioperca) in its Natural Habitats in Poland

1977 ◽  
Vol 34 (10) ◽  
pp. 1581-1585 ◽  
Author(s):  
Maria Nagięć
Keyword(s):  
Key Words ◽  
Primary Productivity ◽  
Thermal Stratification ◽  
Natural Habitats ◽  
Stizostedion Lucioperca

The distribution and biology of pikeperch, Stizostedion lucioperca, in Poland are reviewed along with the characteristics of lakes where pikeperch are abundant. The characteristics of these lakes include low mean depth, lack of thermal stratification in summer, and intensive mixing of water. These characteristics are discussed in relation to primary productivity, zooplankton composition, abundance of benthos, and fish harvests in lakes and firths. Key words: Percidae, pikeperch lakes, harvest, habitat, Stizostedion lucioperca

Immobilization of Bacillus subtilis lipase on a Cu-BTC based hierarchically porous metal–organic framework material: a biocatalyst for esterification

2016 ◽  
Vol 45 (16) ◽  
pp. 6998-7003 ◽  
Author(s):  
Yu Cao ◽  
Zhuofu Wu ◽  
Tao Wang ◽  
Yu Xiao ◽  
Qisheng Huo ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Activity ◽  
Metal Organic Framework ◽  
Porous Metal ◽  
Esterification Reaction ◽  
Hierarchically Porous ◽  
Metal Organic ◽  
First Time ◽  
High Enzymatic Activity ◽  
Organic Framework

Bacillus subtilislipase (BSL2) has been successfully immobilized into a Cu-BTC based hierarchically porous MOF material for the first time. The immobilized BSL2 presents high enzymatic activity and perfect reusability during the esterification reaction.

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