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Production of L(+)-lactic acid, gluc...
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Yu, Roch-chui.
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Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities./
作者:
Yu, Roch-chui.
出版者:
Ann Arbor : ProQuest Dissertations & Theses, : 1990,
面頁冊數:
159 p.
附註:
Source: Dissertation Abstracts International, Volume: 51-04, Section: B, page: 1572.
Contained By:
Dissertation Abstracts International51-04B.
標題:
Food science. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9027053
Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
Yu, Roch-chui.
Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
- Ann Arbor : ProQuest Dissertations & Theses, 1990 - 159 p.
Source: Dissertation Abstracts International, Volume: 51-04, Section: B, page: 1572.
Thesis (Ph.D.)--Cornell University, 1990.
The kinetics of fermenting barley, cassava, corn, oats, and rice directly to L(+)-lactic acid by Rhizopus oryzae NRRL 395 were determined. L(+)-lactic acid production were found to be influenced by the type of substrate, the substrate concentration, the fermentation temperature, and the presence of a neutralizing agent.Subjects--Topical Terms:
3173303
Food science.
Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
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Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
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The kinetics of fermenting barley, cassava, corn, oats, and rice directly to L(+)-lactic acid by Rhizopus oryzae NRRL 395 were determined. L(+)-lactic acid production were found to be influenced by the type of substrate, the substrate concentration, the fermentation temperature, and the presence of a neutralizing agent.
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The mold produced much higher glucoamylase (EC 3.2.1.3) activity from barley, corn, oats, and rice than from cassava. The optimal temperature for enzyme production was 30$\sp\circ$C. Neutralization with CaCO$\sb3$ greatly enhanced the rate of enzyme production. Nitrogen supplementation of cassava resulted in higher enzyme yields.
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The glucoamylase was purified approximately 7-fold by sequential ammonium sulfate fractionation, BioGel P-100, Q-Sepharose, and S-Sepharose. The pH and temperature optima were 4.8 and 60$\sp\circ$C, respectively. Enzyme was stable at temperatures up to 40$\sp\circ$C and at pH values between 3 and 8. The molecular weight was 67,000 daltons as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the pI was 8.7 as determined by chromatofocusing. The K$\sb{\rm m}$ on amylopectin and soluble starch were 0.98 and 1.34 mg/ml, respectively. The V$\sb{\rm max}$ on amylopectin and soluble starch were 782 and 136 units/mg-protein, respectively. The enzyme activity was inhibited by Hg$\sp{++}$, Pb$\sp{++}$, and Cd$\sp{++}$, but not by EDTA.
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An NAD-dependent L(+)-lactate dehydrogenase (EC 1.1.1.27) was purified approximately 175-fold by ammonium sulfate fractionation and chromatofocusing. The purified enzyme was stable at room temperature. The optimal pH was 7.5; the pI as determined by chromatofocusing was 5.2. The molecular weight of native enzyme was 131,000 daltons as estimated by gel filtration, and that of a subunit was 36,000 daltons as determined by SDS-PAGE. Km values for NADH, pyruvate, and 2-oxobutyrate were 1.48, 6.40, and 54.4 $\times$ 10$\sp{-4}$ M, respectively. The enzyme activity was inhibited by Cd$\sp{++}$, Fe$\sp{++}$, Hg$\sp{++}$, Pb$\sp{++}$, and Zn$\sp{++}$, but not by EDTA.
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