Safety evaluation of the food enzyme α‐amylase from the non‐genetically modified Bacillus licheniformis strain TTME 6280 KY [PDF]
EFSA JournalThe food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the non‐genetically modified Bacillus licheniformis strain TTME 6280 KY by Kerry Ingredients & Flavours Ltd.
EFSA Panel on Food Enzymes (FEZ) +16 more
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Utilization of α-amylase (EC 3.2.1.1) resistant maize and pea (Pisum sativum) starch in the rat [PDF]
British Journal of Nutrition, 1989 1. The extent of utilization of α-amylase (EC 3.2.1.1)-resistant retrograded starches in vivo was assessed in male Wistar rats (about 100 g body-weight). All animals were given a fibre-free semi-synthetic basal diet (SS) containing sucrose as the only carbohydrate source, ad lib., for 13 d. On day 14, after an overnight fast, rats were allocated to one
Richard M. Faulks +2 more
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α-Amylase (EC 3.2.1.1) susceptibility rather than viscosity or gastric emptying rate controls plasma responses to starch in healthy humans [PDF]
British Journal of Nutrition, 1990 The relationship between starch α-amylase (EC3.2.1.1) susceptibility, plasma responses and gastric emptying rates has been investigated in humans. Nine randomly chosen healthy subjects were given three carbohydrate test meals (25 g starch or equivalent glucose units): two maize starch pastes with (a) 240 (S24) or (b) 500 (S50) g amylose/kg, and a ...
Francis Bornet +5 more
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The level and origin of amylase (EC 3.2.1.1) in the digestive tract of chicks receiving trypsin inhibitors in their diet [PDF]
British Journal of Nutrition, 1978 1. Amylase (EC 3.2.1.1) activity found in the intestinal tract of chicks posterior to the stomach is of endogenous origin, as amylase in the food is inactivated by the low pH in the stomachs.2. Ingestion of raw soya-bean diet (RSD) or of heated soya-bean diet (HSD) supplemented with trypsin inhibitors induced higher amylase activities in the lower part
Zafrira Nitsan, Zecharia Madar
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Human salivary α‐amylase (EC.3.2.1.1) activity and periodic acid and schiff reactive (PAS) staining: A useful tool to study polysaccharides at an undergraduate level [PDF]
Biochemistry and Molecular Biology Education, 2006 AbstractHealth science education is presently in discussion throughout Europe due to the Bologna Declaration. Teaching basic sciences such as biochemistry in a health sciences context, namely in allied heath education, can be a challenging task since the students of preclinical health sciences are not often convinced that basic sciences are clinically ...
Rúben Fernandes +3 more
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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]
British Journal of Nutrition, 1991 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.
Margaret Longstaff, J. M. McNab
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Seasonal influence on the microbial diversity and flavor substances in the strong flavor Daqu fermentation [PDF]
Food Chemistry: Molecular SciencesBaijiu is highly dependent on open Daqu fermentation, which is easily affected by seasonal fluctuations. This study systematically analyzed winter (WID) and summer (SUD) strong flavor Daqu by integrating physicochemical analysis, microbial community ...
Han Wang +10 more
doaj +2 more sources
Safety evaluation of the food enzyme α‐amylase from the genetically modified Bacillus licheniformis strain DP‐Dzb105 [PDF]
EFSA JournalThe food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase, EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb105 by Genencor International B.V.
EFSA Panel on Food Enzymes (FEZ) +14 more
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Safety evaluation of an extension of use of the food enzyme α‐amylase from the non‐genetically modified Bacillus amyloliquefaciens strain AE‐BAA [PDF]
EFSA JournalThe 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 AE‐BAA by Amano Enzyme Inc.
EFSA Panel on Food Enzymes (FEZ) +16 more
doaj +2 more sources
Safety evaluation of the food enzyme α‐amylase from the genetically modified Bacillus licheniformis strain DP‐Dzb106 [PDF]
EFSA JournalThe food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb106 by Genencor International B.V.
EFSA Panel on Food Enzymes (FEZ) +16 more
doaj +2 more sources