Improving Fatty Extrudate Structure With Amylase and Protease

Pilli, Teresa De; Severini, C.; Carbone, Barbara F.; Giuliani, Roma; Derossi, A.

doi:10.1111/j.1745-4514.2004.04403.x

Cited by 10 publications

(10 citation statements)

References 12 publications

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“…The progressive technological development in the industrial application of amylases evidently indicates that these enzymes continue to draw the attention of industrialists and researchers alike. The screening of new activities and the protein engineering of already existing enzymes have always stimulated the development of new original and interesting functions (Conrad et al 1995;Declerck et al 2002;De Pilli et al 2004;Ben Ali et al 2006). This has been motivated by a determined search for efficient methods that can help direct and better improve the exploitation and utilization of the existing natural biodiversity and the powerful catalytic activities it is endowed with.…”

Section: Introductionmentioning

confidence: 99%

CLONING AND SEQUENCING OF THE α-AMYLASE GENE FROMBACILLUS SUBTILISUS116 STRAIN ENCODING AN ENZYME CLOSELY IDENTICAL TO THAT FROMBACILLUS AMYLOLIQUEFACIENSBUT DISTINCT IN THERMAL STABILITY

Messaoud

Mabrouk

Jemli

et al. 2010

Journal of Food Biochemistry

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The gene encoding for the α‐amylase AMYUS116 was cloned and sequenced. The amino acid sequence of AMYUS116 exhibited an almost perfect homology with the α‐amylase BACAAM, excluding the residues N205 and N217 of AMYUS116 that were changed to H205 and I217 into BACAAM. Three mutant derivatives from AMYUS116 (N205H, N217I and N205H/N217I) were created by site‐directed mutagenesis and their physicochemical and kinetic properties were compared with those of the wild‐type enzymes. Therefore, the undertaken amylases mainly generated maltohexaose from starch and had radically the same kinetic parameters and optimum pH and temperature. They, however, were significantly distinct in thermal stability; AMYUS116 was more thermosensible as its half‐life time at 80C was 13 min, while those of BACAAM and the double mutant were likewise 38 min. The single‐mutant amylases exhibited an identically intermediate thermal stability as their half‐life times at 80C were roughly 22 min. PRACTICAL APPLICATIONS Of particular interest to the current search is that the different thermal stability between AMYUS116 and BACAAM can lead to novel findings pertaining to protein stability, which can bring about new strategies for protein engineering. Basically, the comparative study of closely related amylases and the protein engineering of already existing ones are certainly important because they offer opportunities to understand the structure–function relationships of these biocatalysts.

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Section: Introductionmentioning

confidence: 99%

CLONING AND SEQUENCING OF THE α-AMYLASE GENE FROMBACILLUS SUBTILISUS116 STRAIN ENCODING AN ENZYME CLOSELY IDENTICAL TO THAT FROMBACILLUS AMYLOLIQUEFACIENSBUT DISTINCT IN THERMAL STABILITY

Messaoud

Mabrouk

Jemli

et al. 2010

Journal of Food Biochemistry

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“…The increase in GA amylase amount caused a high dextrination of starch and a consequent reduction of its gelatinization. The increase in GA protease, causing the degradation of gluten in hydrosoluble compounds with low molecular weight, could compete with starch for water absorption (De Pilli et al. 2004).…”

Section: Resultsmentioning

confidence: 99%

“…The 30 combinations obtained for CCD are shown in Table 3. The appropriate range of processing parameters and amounts of enzymes were chosen according to De Pilli et al (2004).…”

Section: Experimental Designmentioning

confidence: 99%

“…In the field of extrusion, the possibility of using an extruder as a “bioreactor” – i.e., to optimize process parameters in order to favor enzymatic reactions – was studied. In particular, De Pilli et al. (2004) studied the effects of two commercially available enzymes (protease and amylase) on the texture of products obtained from wheat and almond flours extruded at low temperature (54C).…”

Section: Introductionmentioning

confidence: 99%

“…In the field of extrusion, the possibility of using an extruder as a "bioreactor" -i.e., to optimize process parameters in order to favor enzymatic reactions -was studied. In particular, De Pilli et al (2004) studied the effects of two commercially available enzymes (protease and amylase) on the texture of products obtained from wheat and almond flours extruded at low temperature (54C). Their results showed that the protease affected the rheological characteristics of dough, with a rapid drop in consistency during farinographic analyses, and that it improved the structure of extrudates with high lipid content (less break strength, high porosity and high water solubility index).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Study on Interaction Among Extrusion‐cooking Process Variables and Enzyme Activity: Evaluation of Extrudate Structure

Pilli

Legrand

Derossi

et al. 2010

J Food Process Engineering

Self Cite

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A blend of wheat flour (moisture content 11.61%) and different amounts of two commercial enzymes like GRINDAMYL (GA) amylase 1000 (0–0.1 g/kg) and GA protease 41 (0–1.0 g/kg) were extruded through a co‐rotating twin‐screw extruder. The effects of barrel temperature (60–120C), dough moisture (20–36%), screw speed (100–400 rpm) and different amounts of enzymes on structure of extrudates (porosity and break strength) were studied using response surface methodology. Results showed that the highest value of porosity (62.47% ± 4.07) was obtained at the highest value of barrel temperature (120C) and at the largest amounts of GA protease 41 (1.0 g/kg) or GA amylase 1000 (0.1 g/kg). However, the simultaneous addition of large amounts of both enzymes caused a negative effect on expansion degree (porosity < 30%). Large amounts of moisture dough and GA amylase 1000 resulted in a high value of break strength (25.7 N/mm2) and in stiff‐textured extrudates. PRACTICAL APPLICATIONS This research could provide some information about the effects of and the interactions between extrusion parameters and enzyme activities, which are commonly used to produce bakery products, in order to improve the texture of extrudates processed at low barrel temperatures, i.e., 60C, for example, extrudates with thermolabile components like vitamins or extrudates with high lipid fraction like breakfast cereals, pet food, etc.

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Mechanoenzymatic Reactions – Challenges and Perspectives

Hollenbach,

Ochsenreither

2023

ChemCatChem

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Mechanoenzymology has emerged as a recent topic in modern research and process design in the transition towards green chemistry. Due to the almost solvent‐free character of mechanoenzymatic reactions solvent usage is considerably reduced and waste can be avoided. Moreover, mechanoenzymatic reactions show highly promising space‐time yields and conversions, however, are still less investigated than their chemical counterparts. The selectivity of enzymes is an important feature for designing green processes and avoiding formation of by‐products. In this review, different mechanoenzymatic strategies are pointed out, involving the most common applied devices, i.e., shaker ball mills, planetary ball mills and twin‐screw extruders. Their compatibility with upscaling and continuous processes is discussed and reusability of enzymes in the different mechanoenzymatic processes is evaluated. In addition, learnings from mechanochemistry are presented and their potential benefits for mechanoenzymology are outlined.

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Improving Fatty Extrudate Structure With Amylase and Protease

Cited by 10 publications

References 12 publications

CLONING AND SEQUENCING OF THE α-AMYLASE GENE FROMBACILLUS SUBTILISUS116 STRAIN ENCODING AN ENZYME CLOSELY IDENTICAL TO THAT FROMBACILLUS AMYLOLIQUEFACIENSBUT DISTINCT IN THERMAL STABILITY

CLONING AND SEQUENCING OF THE α-AMYLASE GENE FROMBACILLUS SUBTILISUS116 STRAIN ENCODING AN ENZYME CLOSELY IDENTICAL TO THAT FROMBACILLUS AMYLOLIQUEFACIENSBUT DISTINCT IN THERMAL STABILITY

Study on Interaction Among Extrusion‐cooking Process Variables and Enzyme Activity: Evaluation of Extrudate Structure

Mechanoenzymatic Reactions – Challenges and Perspectives

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