scholarly journals Determination of Cell Permeabilization and Beta-Galactosidase Extraction from Aspergillus oryzae CCT 0977 Grown in Cheese Whey

2018 ◽  
Vol 2018 ◽  
pp. 1-6
Author(s):  
Caroline dos Santos Viana ◽  
Denise Renata Pedrinho ◽  
Luiz Rodrigo Ito Morioka ◽  
Hélio Hiroshi Suguimoto
Keyword(s):  
Enzymatic Activity ◽  
Aspergillus Oryzae ◽  
Cheese Whey ◽  
Cell Permeability ◽  
Lactose Hydrolysis ◽  
Cell Permeabilization ◽  
Efficient Condition ◽  
Deproteinized Cheese Whey ◽  
Beta Galactosidase

Aspergillus oryzae grown in cheese whey has the ability to produce beta-galactosidase. The objective of this work was to define the parameters for the determination of cell permeabilization and extraction of the enzyme from Aspergillus oryzae CCT 0977 biomass, with high enzymatic activity. The Box–Behnken design was used to determine cell permeabilization and extraction of beta-galactosidase conditions. The fermentation was carried out for a period of 5 days at 28°C, having as substrate the deproteinized cheese whey. To determine the effect of the variables on beta-galactosidase activity, enzymatic activity was determined by the lactose hydrolysis reaction. The most efficient condition for cell permeabilization was 25% ethanol at 30°C for 90 min, obtaining an enzymatic activity of 0.44 U·mL−1. For beta-galactosidase extraction from the biomass, the most efficient condition was 5.3% chloroform at 48°C, with an enzymatic activity of 0.17 U·mL−1. The use of ethanol was most efficient to promote cell permeability of Aspergillus oryzae CCT 0977.

scholarly journals A Comprehensive Bioprocessing Approach to Foster Cheese Whey Valorization: On-Site β-Galactosidase Secretion for Lactose Hydrolysis and Sequential Bacterial Cellulose Production

Fermentation ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. 184
Author(s):  
Iliada K. Lappa ◽  
Vasiliki Kachrimanidou ◽  
Aikaterini Papadaki ◽  
Anthi Stamatiou ◽  
Dimitrios Ladakis ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Bacterial Cellulose ◽  
Cheese Whey ◽  
Initial Moisture Content ◽  
Product Formation ◽  
Added Value ◽  
Aspergillus Awamori ◽  
Lactose Hydrolysis ◽  
Hydrolysis Time ◽  
Strain Specificity

Cheese whey (CW) constitutes a dairy industry by-product, with considerable polluting impact, related mostly with lactose. Numerous bioprocessing approaches have been suggested for lactose utilization, however, full exploitation is hindered by strain specificity for lactose consumption, entailing a confined range of end-products. Thus, we developed a CW valorization process generating high added-value products (crude enzymes, nutrient supplements, biopolymers). First, the ability of Aspergillus awamori to secrete β-galactosidase was studied under several conditions during solid-state fermentation (SSF). Maximum enzyme activity (148 U/g) was obtained at 70% initial moisture content after three days. Crude enzymatic extracts were further implemented to hydrolyze CW lactose, assessing the effect of hydrolysis time, temperature and initial enzymatic activity. Complete lactose hydrolysis was obtained after 36 h, using 15 U/mL initial enzymatic activity. Subsequently, submerged fermentations were performed with the produced hydrolysates as onset feedstocks to produce bacterial cellulose (5.6–7 g/L). Our findings indicate a novel approach to valorize CW via the production of crude enzymes and lactose hydrolysis, aiming to unfold the output potential of intermediate product formation and end-product applications. Likewise, this study generated a bio-based material to be further introduced in novel food formulations, elaborating and conforming with the basic pillars of circular economy.

Comparison of galactooligosaccharides synthesis during lactose hydrolysis by immobilized Aspergillus oryzae beta-galactosidase systems

2015 ◽  
Author(s):  
Ana Elizabeth Cavalcante Fai Buarque de Gusmão ◽  
Haroldo Yukio Kawaguti ◽  
Isabela Thomazelli ◽  
Glaucia Maria Pastore
Keyword(s):  
Aspergillus Oryzae ◽  
Lactose Hydrolysis ◽  
Beta Galactosidase

scholarly journals Saccharomyces fragilis IZ 275 IN CHEESE WHEY CELL PERMEABILIZATION USING DIFFERENT ORGANIC SOLVENTS

2020 ◽  
Vol 9 (9) ◽  
pp. e113996952
Author(s):  
Alessandra Bosso ◽  
Adriana Aparecida Bosso Tomal ◽  
Lucas Caldeirão ◽  
Josemeyre Bonifacio da Silva ◽  
Raul Jorge Hernan Castro-Gomez ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Organic Solvent ◽  
Response Surface ◽  
Organic Solvents ◽  
Large Scale ◽  
Cheese Whey ◽  
Fermentation Medium ◽  
Lactose Hydrolysis ◽  
Cell Permeabilization ◽  
Permeabilized Cells

The aim of this study was to verify the efficacy of different organic solvents, in the permeabilization of Saccharomyces fragilis IZ 275, by using a Central Composite Rotational Design (CCRD) 23 and Response Surface Methodology (RSM). Furthermore, we aimed to evaluate the effectiveness of the permeabilization process by monitoring lactose hydrolysis and obtaining images of non-permeabilized and permeabilized cells by Scanning Electron Microscopy (SEM). The yeast S. fragilis IZ 275 was grown in a fermentation medium composed of cheese whey, and the permeabilized cells was estimated by β-galactosidase activity. The response surface methodology was used as it is an efficient tool to optimize the permeabilization process as well as to identify the organic solvent which was most effective for this process. Our results show that the concentration and type of organic solvent, as well as permeabilization temperature and time influence the cells permeabilization process.. Considering the experimental results, the best conditions when using chloroform are a concentration of 4 % at 25 ºC during 20 min with 81.03 % lactose hydrolysis. In this study, we found that the use of ethanol for cellular permeabilization  lead to obtaining β-galactosidase enzyme, a process which can be used in a large scale by the food industry, being a cheaper and more environmentally safe way of obtaining this enzyme.

A Method for the Colorimetric Determination of β-Glucuronidase in Urine, Serum, Tissue; Assay of Enzymatic Activity in Health and Disease

1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg
Keyword(s):  
Enzymatic Activity ◽  
Colorimetric Determination ◽  
Health And Disease ◽  
Urine Serum

Theoretical substantiation of the cryoscopic method for determination of the degree of lactose hydrolysis in milk whey

2018 ◽  
pp. 19-20
Author(s):  
V.P. Panov ◽  
◽  
M.N. Koverda ◽  
B.G. Gavrilov ◽  
S.A. Kucherenkov ◽  
...  
Keyword(s):  
Lactose Hydrolysis ◽  
Milk Whey ◽  
Theoretical Substantiation

Fluorimetric Determination Of Mercury (Ii) Based On The Inhibition Of The Enzymatic Activity Of Urease

1994 ◽  
Vol 27 (5) ◽  
pp. 867-878 ◽  
Author(s):  
D. W. Bryce ◽  
J. M. Fernández-Romero ◽  
M. D. Luque de Castro
Keyword(s):  
Enzymatic Activity ◽  
Fluorimetric Determination

Determination of fexofenadine in Hank's balanced salt solution by high-performance liquid chromatography with ultraviolet detection: application to Caco-2 cell permeability studies

2014 ◽  
Vol 29 (4) ◽  
pp. 537-544 ◽  
Author(s):  
Marco Antônio dos. Reis Júnior ◽  
Ana Cláudia Miranda de Faria ◽  
Eudes da. Silva Velozo ◽  
Teresa Dalla Costa ◽  
Frank Pereira de Andrade ◽  
...  
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Salt Solution ◽  
High Performance ◽  
Cell Permeability ◽  
Ultraviolet Detection ◽  
Permeability Studies

scholarly journals A rapid direct assay for the determination of the separate activities of the three arylsulphatases of Aspergillus oryzae

1977 ◽  
Vol 166 (3) ◽  
pp. 411-413 ◽  
Author(s):  
G R J Burns ◽  
C H Wynn
Keyword(s):  
Phenolic Compounds ◽  
Aspergillus Oryzae ◽  
Substrate Specificities ◽  
Direct Assay ◽  
Assay Procedure ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Potential Use

1. The three arylsulphatases of Aspergillus oryzae exhibit pronounced kinetic differences and substrate specificities. Arylsulphatase I hydrolyses all substrates tested, whereas arylsulphatase III will not hydrolyse tyrosine O-sulphate or phenolphthalein disulphate. Arylsulphatase II does not hydrolyse p-nitrophenyl sulphate or phenolphthalein disulphate at appreciable rates in the absence of added phenolic compounds. Phenols such as tyramine increase the rate of hydrolysis of these substances by this enzyme 1000-fold. At pH 6.9 arylsulphatase I exhibits an apparent Km of 0.1 mM for p-nitrophenyl sulphate, whereas the Km of arylsulphatase III for this substrate is 1 mM. 2. These differences were utilized to develop an assay procedure which can be used to determine the separate activities of the three enzymes present in mixtures. This assay has potential use as a means of examining the relative activities of the three enzymes in investigations of the differences in the mechanisms regulating their synthesis.

scholarly journals Chlorella sorokiniana cultivation in cheese whey for β-galactosidase production

2021 ◽  
Vol 10 (12) ◽  
pp. e468101220727
Author(s):  
Maicon Jhonatan Bueno do Amaral Santos ◽  
Diva de Souza Andrade ◽  
Alessandra Bosso ◽  
Mayara Mari Murata ◽  
Luiz Rodrigo Ito Morioka ◽  
...  
Keyword(s):  
Physicochemical Parameters ◽  
Cheese Whey ◽  
High Capacity ◽  
Chlorella Sorokiniana ◽  
Cultivation Condition ◽  
High Biomass ◽  
Box Behnken Design ◽  
Biomass Yields ◽  
Biotechnological Processes ◽  
Beta Galactosidase

Biotechnological processes with microalgae with the aim to achieve high biomass yields must choose the appropriate nutrients and physicochemical parameters, taking into account the specific characteristics of each species to determine the basic needs for its growth. In the present study, the better growth condition of Chlorella sorokiniana IPR 7104 was optimized to reach the maximum beta-galactosidase production. The cheese whey concentration (%), temperature (˚C) and pH were factors investigated and a Box-Behnken Design (BBD) approach was implemented using Statistica 7.0 software. We observed that the cultivation condition to Chlorella sorokiniana IPR 7104 was the heterotrophic, which showed the major enzymatic activity, consequently a lower residual lactose content. Under heterotrophic conditions (without light) the β-galactosidase activity increased linearly until the 8th day. Biomass production grew linearly on the 12th day. The microalgae consumed 89.6% of lactose in 3 days, showing a high capacity to metabolize this disaccharide, through β-galactosidase synthesis. The maximum β-galactosidase production by Chlorella sorokiniana IPR 7104, in heterotrophic conditions and using cheese whey as carbon source, is obtained using the following conditions: 30°C temperature, concentration of ethanol at 20% and time of 4 min.

scholarly journals Immobilization of Isolated Lipase From Moldy Copra(Aspergillus Oryzae)

2011 ◽  
Vol 8 (2) ◽  
pp. 896-902
Author(s):  
Seniwati Dali ◽  
A. B. D. Rauf Patong ◽  
M. Noor Jalaluddin ◽  
Pirman ◽  
Baharuddin Hamzah
Keyword(s):  
Thermal Stability ◽  
Aspergillus Oryzae ◽  
Immobilized Lipase ◽  
Optimum Temperature ◽  
Adsorption Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Recovery Technique ◽  
Free Lipase

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

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