Milk-Coagulating Extract Produced from Solanum aethiopicum Shum Fruits: Multivariate Techniques of Preparation, Thermal Stability and Effect on Milk Solids Recovery in Curd

Abstract This study investigated a novel procedure of Solanum aethiopicum Shum fruits extract (SASFE) preparation using multivariate experimental designs as factorial and Box–Behnken. The thermal stability of optimized extract as well as its influence on the milk solids in curd was determined. The results showed that extraction time, fruit maturity and pH did not affect significantly SASFE preparation, while the amount of fruits, extraction temperature and NaCl concentration of extractant had a significant effect (p < 0.05). The greatest coagulant index was obtained under the following conditions: 12.5% of fruits, 25°C of extraction temperature and 4% NaCl concentration of extractant. It was thermosensitive and exhibited optimum temperature at 50°C. There was no statistical difference between SASFE and calf rennet in terms of solids yield in curd, estimated yield and actual yield. On the basis of these results, SASFE can be used as a vegetable alternative to calf rennet.

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THE EFFECTS OF TEMPERATURE UPON PANCREATIC AMYLASE IN SELECTED REPTILES AND AN AMPHIBIAN

Canadian Journal of Zoology ◽

10.1139/z67-029 ◽

1967 ◽

Vol 45 (2) ◽

pp. 227-232 ◽

Cited By ~ 3

Author(s):

Yvette Abrahamson ◽

Michael Maher

Keyword(s):

Thermal Stability ◽

Amylase Activity ◽

Effect Of Temperature ◽

Maximum Temperature ◽

Pancreatic Amylase ◽

Optimum Temperature ◽

Preferred Temperatures ◽

Effects Of Temperature ◽

Subcellular Level ◽

Thermal Stability Of

The effect of temperature on pancreatic amylase was studied on three species of reptiles and one amphibian. Pancreata were removed from the animals, homogenized, and assayed for amylase activity by the Caraway procedure. Assays were conducted at various temperatures to determine the optimum temperature of activity and the maximum temperature for thermal stability of pancreatic amylase. It appears that between reptiles and amphibians, and also among species of reptiles, there are thermally dependent differences at the subcellular level which are similar to the differences in the preferred temperatures of the animals.

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IMMOBILIZATION OF PAPAIN ON CHITOSAN

Indonesian Journal of Chemistry ◽

10.22146/ijc.21609 ◽

2010 ◽

Vol 8 (3) ◽

pp. 372-376

Author(s):

Sari Edi Cahyaningrum ◽

Narsito Narsito ◽

Sri Juari Santoso ◽

Rudiana Agustini

Keyword(s):

Thermal Stability ◽

Optimum Temperature ◽

Ph Optimum ◽

Optimum Ph ◽

Thermal Stability Of

In this study, papain was immobilized on chitosan with Mg(II) cosslinked agent. Studies on free and immobilized papain systems for determination of optimum pH, optimum temperatur, thermal stability and reusability were carried out. The results showed that free papain had optimum pH 6.5 and optimum temperature 55 °C while the immobile papain hadoptimum pH 8 and optimum temperature 80 °C. The thermal stability of the immobilized papain, relative to that of the free papain, was markedly increased. The immobilized papain can be reused for at least six times. Keywords: papain, immobilization, chitosan

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Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Mediterranean Journal of Chemistry ◽

10.13171/mjc10202002131126ysh ◽

2020 ◽

Vol 10 (2) ◽

pp. 155-161

Author(s):

Yandri Yandri ◽

Tati Suhartati ◽

Heri Satria ◽

Arum Widyasmara ◽

Sutopo Hadi

Keyword(s):

Thermal Stability ◽

Bacillus Subtilis ◽

Half Life ◽

Thermodynamic Data ◽

Immobilized Enzyme ◽

Residual Activity ◽

Optimum Temperature ◽

Chitosan Matrix ◽

T Values ◽

Thermal Stability Of

In this research, the immobilization of α-amylase from Bacillus subtilis ITBCCB148 by crosslinking method on chitosan matrix has been performed. This research aims to know the effect of immobilization on the thermal stability of α-amylase. The results showed that the native α-amylase has an optimum temperature of 65oC, KM = 1.6 mg mL-1 substrate, and Vmax = 39.7 µmol mL-1 min-1. The immobilized α-amylase has optimum temperature of 75oC, KM = 3.5 mg mL-1 substrate, and Vmax = 7.05 µmol mL-1 min-1. The residual activity of the native and immobilized enzyme on thermal stability test at 65oC for 80 minutes was 58% and 86.15%, respectively. The immobilized enzyme can be reused up to six repeated cycles.The thermodynamic data of native enzyme was t½ = 113.6 min, ki = 6.1x10-3 min-1, and ΔGi = 107.3 kJ mol-1, while the immobilized enzyme was t½ = 433.1 min, ki= 1.6x10-3 min-1, and ΔGi 111.1 kJ mol-1. Based on the decrease of ki, and the increase of ΔGi and half-life(t½) values, the immobilization of α-amylase with chitosan can increase the thermal stability of this enzyme.

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Peningkatan Stabilitas Termal Enzim α-Amilase dari Bacillus subtilis ITBCCB148 dengan Amobilisasi Menggunakan Zeolit

Talenta Conference Series Science and Technology (ST) ◽

10.32734/st.v2i2.561 ◽

2019 ◽

Vol 2 (2) ◽

Author(s):

Yandri ◽

Fathaniah Sejati ◽

Tati Suhartati

Keyword(s):

Thermal Stability ◽

Bacillus Subtilis ◽

Immobilized Enzyme ◽

Specific Activity ◽

Residual Activity ◽

Stability Test ◽

Optimum Temperature ◽

Before And After ◽

Cation Exchange Column ◽

Thermal Stability Of

The objective of the research is to increase the thermal stability of -amylase from Bacillus subtilis ITBCCB148 by immobilization using zeolite. For that reason, firstly we need to produce, isolate, and purify the enzyme. The purification of the enzyme was conducted by the following steps: fractionation with ammonium sulphate, dialysis, and CM-cellulose cation exchange column chromatography. The purified enzyme was immobilized using zeolite. The success in immobilization of the enzyme was evaluated by comparing the thermal stability of the enzyme before and after immobilization. Activity of α-amylase was determined by the Mandels and Fuwa method. The protein content was determined based on the method by Lowry. The results showed that the specific activity of purified enzyme was 2473.7 U / mg, increased 19 times compared to crude extract of enzyme having specific activity of 1285.9 U / mg. The purified enzyme has the optimum temperature at 65ºC, while the immobilized enzyme has the optimum temperature at 75ºC. The thermal stability test of the purified enzyme at 65ºC for 100 minutes showed the purified enzyme having residual activity of 20%; t 1 / 2 = 30 min, k i = 0.023 min -1 and ΔGi = 103.65 kJ mol -1 . The thermal stability test of the immobilized enzyme at 65ºC for 100 minutes showed that the immobilized enzyme had residual activity of 40%; t 1/ 2 = 49 min, k i = 0.014 min -1 and ΔGi = 105.03 kJ mol -1 . Immobilization using zeolite has succeeded in increasing the thermal stability of enzyme by 1.64 times compared to the purified enzyme, which is indicated by the decreasing of k i value, the increase of half-life and denaturation energy change (ΔGi).

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The Ordered Phase Formation in Ti-Al-Ga Alloys

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100069193 ◽

1970 ◽

Vol 28 ◽

pp. 440-441

Author(s):

Shiro Fujishiro ◽

Harold L. Gegel

Keyword(s):

Thermal Stability ◽

High Temperature ◽

Titanium Alloys ◽

Growth Kinetics ◽

Stoichiometric Composition ◽

Good Potential ◽

Alpha Titanium ◽

Cold Rolled ◽

Kinetics Of ◽

Thermal Stability Of

Ordered-alpha titanium alloys having a DO19 type structure have good potential for high temperature (600°C) applications, due to the thermal stability of the ordered phase and the inherent resistance to recrystallization of these alloys. Five different Ti-Al-Ga alloys consisting of equal atomic percents of aluminum and gallium solute additions up to the stoichiometric composition, Ti3(Al, Ga), were used to study the growth kinetics of the ordered phase and the nature of its interface.The alloys were homogenized in the beta region in a vacuum of about 5×10-7 torr, furnace cooled; reheated in air to 50°C below the alpha transus for hot working. The alloys were subsequently acid cleaned, annealed in vacuo, and cold rolled to about. 050 inch prior to additional homogenization

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Microstructure studies of tungsten silicide schottky contacts on Gaas

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100126445 ◽

1987 ◽

Vol 45 ◽

pp. 328-329

Author(s):

Yih-Cheng Shih ◽

E. L. Wilkie

Keyword(s):

Thermal Stability ◽

Field Effect Transistors ◽

Schottky Contact ◽

Schottky Contacts ◽

Excellent Thermal Stability ◽

Barrier Heights ◽

Gaas Substrates ◽

Film Adhesion ◽

Threshold Voltages ◽

Thermal Stability Of

Tungsten silicides (WSix) have been successfully used as the gate materials in self-aligned GaAs metal-semiconductor-field- effect transistors (MESFET). Thermal stability of the WSix/GaAs Schottky contact is of major concern since the n+ implanted source/drain regions must be annealed at high temperatures (∼ 800°C). WSi0.6 was considered the best composition to achieve good device performance due to its low stress and excellent thermal stability of the WSix/GaAs interface. The film adhesion and the uniformity in barrier heights and ideality factors of the WSi0.6 films have been improved by depositing a thin layer of pure W as the first layer on GaAs prior to WSi0.6 deposition. Recently WSi0.1 has been used successfully as the gate material in 1x10 μm GaAs FET's on the GaAs substrates which were sputter-cleaned prior to deposition. These GaAs FET's exhibited uniform threshold voltages across a 51 mm wafer with good film adhesion after annealing at 800°C for 10 min.

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