Results 21 to 30 of about 740,354 (168)
Characterising EC regulation: emulation, innovation, re-regulation [PDF]
The thesis characterises European Community (EC) regulation in terms of three levels of ideas, namely that: (a) the EC regulatory process is best understood by particular styles or processes of regulation that the thesis terms emulation, innovation and ...
Matthews, DN, LSE
core +4 more sources
The effect of concentration of tannin-rich bean hulls (Vicia fabaL.) on activities of lipase (EC3.1.1.3) and α-amylase (EC3.2.1.1) in digesta and pancreas and on the digestion of lipid and starch by young chicks [PDF]
The effect of different concentrations of tannin-rich field-bean (Vicia fabaL.) hulls at 0, 20, 50, 150 and 300 g/kg dietary inclusion on the activities of lipase (EC3.1.1.3) and α-amylase (EC3.2.1.1) in digesta and pancreas and on the digestion of lipid and starch was studied in 2–3-week-old male broiler chicks.
M A, Longstaff, J M, McNab
openaire +2 more sources
A brotação da nogueira é dependente da mobilização de carboidratos do lenho para as gemas localizadas na porção superior dos ramos. O objetivo do trabalho foi contribuir para o entendimento do mecanismo de brotação acrótona da nogueira, em clima ...
Idemir Citadin +3 more
doaj +1 more source
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the non‐genetically modified microorganism Bacillus amyloliquefaciens strain BA by HBI Enzymes Inc.
EFSA Panel on Food Contact Materials; Enzymes and Processing Aids (CEP) +24 more
doaj +1 more source
بهینهسازی تولید آنزیم آمیلاز در باکتری مقاوم به سرمای sp. ATR812 Janthinobacterium با استفاده از روشResponse Surface Methodology [PDF]
آمیلاز (EC 3.2.1.1) یکی از مهمترین آنزیم های صنعتی است که کاربردهای گستردهای در صنایع مختلف دارد. این آنزیم پیوند گلیکوزیدی (4-1) α را در نشاسته هیدرولیز کرده و محصولاتی با وزن مولکولی کمتر مثل گلوکز، مالتوز و مالتوتریوز تولید میکند.
راضیه قاضی بیرجندی +3 more
doaj +1 more source
Efficient inactivation of microbial α-amylases (EC 3.2.1.1) can be a challenge in starch systems as the presence of starch has been shown to enhance the stability of the enzymes.
Signe Schram Zinck +4 more
doaj +1 more source
Energy balance and energy values of α-amylase (EC 3. 2. 1. 1)-resistant maize and pea (Pisum sativum) starches in the rat [PDF]
Apparent and partial digestible energy values for α-amylase (EC 3. 2. 1. 1)-resistant, retrograde starches, isolated from cooked maize and pea starches (RMS and RPS respectively), were determined in male Wistar rats (about 180 g) during a 28–29 d balance period with ten animals per treatment. The starches were provided as supplements (100 g/kg diet) to
G, Livesey +4 more
openaire +2 more sources
The food enzyme α‐amylase (4‐α‐d‐glucan glucohydrolase; EC 3.2.1.1) is produced with the genetically modified B. amyloliquefaciens strain DP‐Czb53 by Danisco US Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +23 more
doaj +1 more source
The response to selection in Glycoside Hydrolase Family 13 structures: A comparative quantitative genetics approach. [PDF]
The Glycoside Hydrolase Family 13 (GH13) is both evolutionarily diverse and relevant to many industrial applications. Its members hydrolyze starch into smaller carbohydrates and members of the family have been bioengineered to improve catalytic function ...
Jose Sergio Hleap, Christian Blouin
doaj +1 more source
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase, EC 3.2.1.1) and 1,4‐α‐glucan 6‐α‐glucosyltransferase ((1→4)‐α‐d‐glucan:(1→4)‐α‐d‐glucan(d‐glucose) 6‐α‐d‐glucosyltransferase, EC 2.4.1.24) is produced with a Paenibacillus alginolyticus by ...
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +24 more
doaj +1 more source

