東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Production of L(+)-lactic acid, gluc...

Yu, Roch-chui.

Linked to FindBook

Google Book

Amazon

博客來

Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities./
Author:	Yu, Roch-chui.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 1990,
Description:	159 p.
Notes:	Source: Dissertation Abstracts International, Volume: 51-04, Section: B, page: 1572.
Contained By:	Dissertation Abstracts International51-04B.
Subject:	Food science. -
Online resource:	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.
LDR:03025nmm a2200301 4500 001 2121876
005 20170821084144.5
008 180830s1990 ||||||||||||||||| ||eng d
035 $a (MiAaPQ)AAI9027053
035 $a AAI9027053
040 $a MiAaPQ $c MiAaPQ
100 1 $a Yu, Roch-chui. $3 3283819
245 1 0 $a Production of L(+)-lactic acid, glucoamylase, and lactate dehydrogenase by Rhizopus oryzae from agricultural commodities.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 1990
300 $a 159 p.
500 $a Source: Dissertation Abstracts International, Volume: 51-04, Section: B, page: 1572.
502 $a Thesis (Ph.D.)--Cornell University, 1990.
520 $a 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.
520 $a The mold produced much higher glucoamylase (EC 3.2.1.3) activity from barley, corn, oats, and rice than from cassava. The optimal temperature for enzyme production was 30$\sp\circ$C. Neutralization with CaCO$\sb3$ greatly enhanced the rate of enzyme production. Nitrogen supplementation of cassava resulted in higher enzyme yields.
520 $a The glucoamylase was purified approximately 7-fold by sequential ammonium sulfate fractionation, BioGel P-100, Q-Sepharose, and S-Sepharose. The pH and temperature optima were 4.8 and 60$\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.
520 $a 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.
590 $a School code: 0058.
650 4 $a Food science. $3 3173303
650 4 $a Microbiology. $3 536250
690 $a 0359
690 $a 0410
710 2 $a Cornell University. $3 530586
773 0 $t Dissertation Abstracts International $g 51-04B.
790 $a 0058
791 $a Ph.D.
792 $a 1990
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9027053