• Title/Summary/Keyword: acid-hydrolysed soybean protein

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Esterase Production and Culture Characteristics of Bacteria Isolated from Acid Hydrolysed Soybean Protein (산분해 대두 단백질로부터 분리된 Esterase 생성균의 생육 및 효소생성 특성)

  • Oh, Nam-Soon
    • Applied Biological Chemistry
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    • v.40 no.6
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    • pp.484-489
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    • 1997
  • The characteristics of growth and esterase activity of bacterial strains isolated from acid hydrolysed soybean protein were examined. All the isolated strains having decomposition activity of p-hydroxybenzoic acid butyl ester and esterase producing activity were identified as Bacillus sp. by morphological and biochemical methods. The specific growth rates, esterase activities and p-hydroxybenzoic acid butyl ester decomposition activities of isolated strains were $0.844{\sim}1.213\;h^{-1}$, $21{\sim}222\;mU/ml$ and $5.4{\sim}8.1\;mU/ml$, respectively. In the fermentation of Bacillus sp. KB8 strain which had the highest esterase producing activity, growth, extracellular excretion and intracellular synthesis of esterase were inhibited by adding NaCl in the culture broth. Esterase producing activity gradually increased after late exponential growth phase, until maximum value of 420 mU/ml reached after 64 hours culture period. Esterase of Bacillus sp. KB8 strain was stable up to $50^{\circ}C$ for 30 minutes, but was inactivated by heating for 30 minutes at $70^{\circ}C$. The enzyme activity exponentially decreased during the incubation time at the temperatures of $60^{\circ}C$ and $65^{\circ}C$.

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Angiotensin-I Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Food Proteins (식품단백질 효소가수분해물의 Angiotensin-I 전환효소 저해작용)

  • 염동민;노승배;이태기;김선봉;박영호
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.22 no.2
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    • pp.226-233
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    • 1993
  • Enzymatic hydrolysates of food proteins (defatted soybean cake, egg albumin and casein) were tested for inhibitory activity against angiotensin-I converting enzyme (ACE). Food proteins were hydrolysed with complex enzyme, bromelain, alcalase, $\alpha$-chymotrypsin, trypsin, papain and pepsin by heating method. The hydrolysates obtained from the treatment of complex enzyme and bromelain showed the higher ACE inhibitory activity. ACE inhibitory activity of hydrolysates exhibited a tendency to be increased until 8hrs and increased with increment of concentration. The activity was also stable by heat treatment at 10$0^{\circ}C$ for 20min. Molecular weight of active fraction was about 1, 400 and defatted soybean cake hydrolysate below 1, 400 in case of defatted soybean cake hydrolysate treated with alcalase. Amino acid of the active fractions was abundant in Asp, Glu, Lys, lle, Leu, Ala and Val.

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