Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Tavano, Olga Luisa; Fernández-Lafuente, Roberto; Goulart, Antônio José; Monti, Rubens

doi:10.1016/j.procbio.2013.05.009

Cited by 57 publications

(29 citation statements)

References 35 publications

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“…The slower hydrolysis rate using immobilized trypsin was expected, and appears to be more related to diffusional problems of substrates, as described previously, than environmental conditions. As it is known, K m value can increase due to restricted diffusion of substrate or the high structural rigidity of immobilized enzyme (RODRIGUES et al, 2013;TAVANO et al, 2013). HOMAEI and co-workers (2010) observed a slight increase in K m value when papain was immobilized in cyanogen bromide activated Sepharose.…”

Section: Resultsmentioning

confidence: 99%

Hydrolysis of casein and β-lactoglobulin by immobilized papain after pre-treatment with immobilized trypsin

Pessato¹,

Tavano²

2015

Acta Alimentaria

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Protein hydrolysis using immobilized proteases may present problems, which are mainly caused by the diffusion of macromolecular substrate. Pre-hydrolysed substrate could be a viable alternative in this process. The aim of this work was to test the casein and β-lactoglobulin hydrolysis using immobilized papain on glyoxyl-agarose, following substrate pre-treatment with immobilized trypsin. Although immobilized papain showed diffi culties to degrade the milk proteins, after 10 min of trypsin pre-hydrolysis, the immobilized papain was able to achieve the maximum degree of hydrolysis in shorter time. For pre-hydrolysate casein, the immobilized papain reached 98.9% at 60 min total reaction (including the 10 min pre-digestion). As for β-lactoglobulin, immobilized papain was capable of achieving maximum levels after just 60 min of reaction, where the free enzyme only achieved 60% of its maximum. Pre-hydrolysis with trypsin appears to have worked well as a pre-treatment method to increase the proteolytic action of immobilized papain.

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Section: Resultsmentioning

confidence: 99%

Hydrolysis of casein and β-lactoglobulin by immobilized papain after pre-treatment with immobilized trypsin

Pessato¹,

Tavano²

2015

Acta Alimentaria

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“…Vretblad and Axen [66] reported a global yield of 35% for barley β-amylase covalently attached on Sepharose activated with 4,4 -methylene dianiline. Tavano et al [69] reported global yield of 21% for sweet potato β-amylase immobilized on glyoxyl-agarose support. These results are much closer to those obtained in our work for barley β-amylase ionically adsorbed on chitosan (Table 1).…”

Section: Optimization Of β-Amylase Immobilization Using Cleas Technologymentioning

confidence: 99%

“…The study of the effect of the reaction pH and temperature on the enzyme activity of β-amylase was performed using free enzyme, CLEA-β-BSA-5 and CLEA-β-SPI-12 to investigate the influence of the enzyme immobilization technique on enzyme response to the medium [68][69][70][71] (Figure 2). …”

Section: Effects Of Ph and Temperature On The Activity And The Stabilmentioning

confidence: 99%

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Maltose Production Using Starch from Cassava Bagasse Catalyzed by Cross-Linked β-Amylase Aggregates

et al. 2018

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Barley β-amylase was immobilized using different techniques. The highest global yield was obtained using the cross-linked enzyme aggregates (CLEA) technique, employing bovine serum albumin (BSA) or soy protein isolate (SPI) as feeder proteins to reduce diffusion problems. The CLEAs produced using BSA or SPI showed 82.7 ± 5.8 and 53.3 ± 2.4% global yield, respectively, and a stabilization effect was observed upon immobilization at neutral pH value, e.g., after 12 h at 55 • C, the free β-amylase is fully inactivated, while CLEAs retained 25 and 15% of activity (using BSA and SPI, respectively). CLEA using SPI was selected because of its easier recovery, being chosen to convert the residual starch contained in cassava bagasse into maltose. This biocatalyst permitted to reach almost 70% of maltose conversion in 4 h using 30.0 g/L bagasse starch solution (Dextrose Equivalent of 15.88) and 1.2 U of biocatalyst per gram of starch at pH 7.0 and 40 • C. After 4 reuses (batches of 12 h) the CLEA using SPI maintained 25.50 ± 0.01% of conversion due to the difficulty of recovering.

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“…The encapsulation efficiency is enhanced on the further addition of 2% (w/v) silica gel. Glyoxyl and glutatraldehyde supports can also be used for the stabilization of the enzyme by multipoint attachment (Tavano et al, 2013). Thus the most important aspect that has to be considered when immobilizing the amylase is the huge size of the substrate that cannot penetrate through the pores of the gel resulting in an inadequate accessibility of the enzyme to the substrate.…”

Section: Biofilm Removal Efficacymentioning

confidence: 99%

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Sachdev

Ojha

Mishra

2016

Int J Appl Sci Biotechnol

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Amylase is one of the leading enzymes used in industry from decades. The preliminary function of this enzyme is the hydrolysis of the starch molecule into glucose units and oligosaccharides. Amylases have spectacular application in broad spectrum of industries such as food, detergent, pharmaceutical and fermentation industries. Among different type of amylases α-amylase is in utmost demand because of its striking features. This particular enzyme is a good substitute over the chemicals catalyst used in industries. α-amylases can be acquired from different sources such as microorganism, animals and plants. Microorganisms are the major source of production of amylase because of the ease of availability, manipulation and operation. The starch converting enzymes is basically generated using submerged fermentation. Some of the prominent characteristics of amylase are its mode of action, substrate specificity and operating condition (temperature and pH). Amylases from different bacterial sources contribute differently to the particular trait of the enzyme. Bacillus amylases have been studied and applied so far because of their robustness in nature and easy accessible pure form of it. Thus this makes it more specific and fit for distinct application in the industry. The purpose of this manuscript was the comparative analysis of the physical and chemical features of α amylases from Bacillus species. It also focuses on the unique characteristics of this enzyme and their industrial applications.

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Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Cited by 57 publications

References 35 publications

Hydrolysis of casein and β-lactoglobulin by immobilized papain after pre-treatment with immobilized trypsin

Hydrolysis of casein and β-lactoglobulin by immobilized papain after pre-treatment with immobilized trypsin

Maltose Production Using Starch from Cassava Bagasse Catalyzed by Cross-Linked β-Amylase Aggregates

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

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