Studies on the .ALPHA.-glucoside hydrolase inhibitor, adiposin. III. .ALPHA.-Glucoside hydrolase inhibitory activity and antibacterial activity in vitro.
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Glucoside
Alpha-glucosidase
Gram-Negative Bacteria
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Mosquitofish
Digestive enzyme
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Abstract The contribution of α‐ and β‐amylases to the production of sugars fermentable in bread fermentation has been followed by measuring the gassing power of pregelatinised wheat starch mixed with a buffered solution of yeast nutrients and a yeast suspension. After crystalline amylases were added, β‐amylase contributed at least 10 times more fermentable sugars than equal amounts of bacterial, pancreatic or fungal amylases. Among the α‐amylases, the enzyme of bacterial origin was the most potent; the fungal, the least; and the pancreatic, intermediate. Mixtures of α‐ and β‐amylases gave fermentable sugars in amounts slightly smaller than calculated. Mixtures of crude preparations from cereals showed a response to β‐amylase, provided the plant α‐amylase was low in β‐amylase.
Yeast extract
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Electrophoretical and biochemical characteristics of amylase in the extracts of lung tissues were investigated.Amylase activity in the extracts of the diseased lung tissues was significantly higher than in the normal lung tissues. However, electrophoretical properties of amylase in these tissues were revealed to be the same as salivary amylase on polyacrylamide gel electrophoresis.Heat treatment at 56°C demonstrated that amylase in the extracts of lung tissues was more stable than that of saliva or pancreatic juice.Amylase activity in saliva and the extracts of lung tissues was suppressed similarly by rabbit antiserum against human salivary amylase.Km value of amylase in the extracts of lung tissues for Blue Starch was almost same as that of saliva, indicating that both have the same enzymatic nature.
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Amylase and xylanase enzyme concentrations in the pancreas, small intestine, and crop were measured in Nicholas male poults fed diets with and without supplemental amylase and xylanase from 0 to 8 wk of age. Eight birds from each of three diets (control, amylase-supplemented, xylanase-supplemented) were killed every 3 d to determine the amylase and xylanase activity within the pancreas, small intestine, and crop. Pancreatic organ weight was not affected by diet, indicating an absence of dietary amylase effect upon pancreatic tissue growth. Pancreatic amylase activity was not consistently affected by diet. Amylase activity within the intestinal chyme increased sporadically with dietary amylase supplementation over the control and xylanase-supplemented diets. Increasing supplemental amylase activity levels may provide more conclusive evidence of an additive effect of dietary amylase and endogenous amylase activity. Xylanase supplementation within the feed did not affect endogenous amylase activity.
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To determine theα,β-amylase activity and total amylase activity in 25radish varieties,field experiments used randomized block design and repeated 3times,α?amylase,β-amylase and total amylase activity were estimated by the 3,5-dinitrosalicylic acid method after fleshy root harvest,for providing a reference and establishment relationship of α?amylase,β-amylase and total amylase activity.The results showed that there were significance differences ofα?amylase,β-amylase and total amylase activity in different radish varieties;the A04,S01,A17,A20,S05and A07were the higher α?amylase activity and the A19,A06,A17,A12and S03were the the higher β-amylase and total amylase activity.The ratio ofα,β-amylase activity in total amylase activity was 8.11%to 25.57% and 75.26%～91.89%,respectively and the relationship of them was Y Total amylase activity =-0.029+1.039X α-amylase activity +0.998X β-amylase activity.
Raphanus
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Chromogenic
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ABSTRACT ℓ-Menthyl-6′-O-acetyl-β-D-glucoside has been isolated and characterized as a new constituent of a leaf extract of "Wasenami," a Japanese cultivar of Mentha arvensis L. var. piperascens Malinv. Its structure was confirmed by 13C-NMR. β-Sitosteryl-β-D-glucoside and ℓ-menthyl-β-D-glucoside were also isolated and characterized along with the 6′-O-acetyl derivative.
Glucoside
Monoterpene
Mentha arvensis
Derivative (finance)
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Alpha-amylase
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퇴비 숙성초기에 고온성 cellulose 분해이용균으로 분리된 Herpetosiphon geysericola CUM 317균주는 전분분해 효소인 α-amylase, β-amylase 및 glucoamylase를 모두 생성한다. 이 균을 사용하여 그 배양조건을 달리하여 각 amylase의 생성관계를 서로 비교한바 50℃의 밀기울 고체배지나 40℃의 액체배지상에서 β-amylase는 배양초기 10시간만에 최대의 생성력가를 보였는 반면, α-amylase와 glucoamylase는 30 내지 40시간 정도의 배양말기에 최대를 이루었다. Polypeptone을 함유한 액체배지에 탄소원의 첨가나 무기질소원의 첨가는 전반적으로 amylase들의 생성이 크게 저하되었으나 cellulose에 의해서 glucoamylase의 경우 150% 정도 증가되었다. 액체배지에 Cu SO₄를 첨가해 줌으로서 α-amylase만의 생성증가 효과를 얻었고 CdSO₄에 의하여 β-amylase만의 생성증가가 있었으며, 그리고 CaCl₂에 의하여 glucoamylase만의 증가효과가 있은 반면, 상대적으로 β-amylase의 급격한 감소가 일어났다. 이들 amylase들의 최적 효소생성 pH는 7.5였으며, 최적온도는 α-amylase와 glucoamylase의 경우 40℃였고 β-amylase는 30℃였다.
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