蓝湿皮酶软化的特性研究

以自行研制的一种复合酶为软化剂 ,研究了 p H值、反应温度、反应时间、酶用量以及铬含量对猪蓝湿皮软化效果的影响 ,其软化效果以软化液中羟脯氨酸的浓度增量来表征。研究结果表明 :通过蓝湿皮软化来改善成品革的质量是可行的 ,而且有明显的效果 ;以软化液中羟脯氨酸的浓度来表征软化效果是一个有效的方法 ;当用该复合酶软化猪蓝湿皮时 ,最适 p H值范围为 6 .0 - 6 .5 ;反应温度在 4 0 - 6 5℃之间时 ,软化效果随温度的升高而增大 ;在 5 5℃条件下 ,该酶有很好的热稳定性 ,能长时间保持活力不衰减 ;最适酶用量为 30 0 U/ g试样 ;蓝湿皮的铬含量对软化效果有影响 ,用该方法处理的蓝湿皮 ,其铬离子质量含量一般应≤ 2 .5 %。     

大豆浸出毛油脱胶新工艺

对大豆浸出毛油脱胶工艺路线中的膜除杂工艺、酶解法脱胶工艺进行了研究,并对影响酶解法脱胶工艺的主要因素进行了单因素实验,同时对各主要因素对该工艺的综合影响进行了正交优化,得出了该工艺的主要影响因素在该工艺中的最佳操作条件,即酶解4h、水化1.25h、预热温度为70℃、酶用量0.35g/750mL毛油.     

Reaction steady states and stationary states in modelling semi-batch enzyme hydrolysis

Dimensionless material balance equations describing an uninhibited enzyme hydrolysis process in a semi-batch reactor (i.e. fed-batch reactor) are formulated; numerical solution of these equations provided concentration profiles of the enzyme-substrate complex by using published kinetic parameters. The unrestricted values obtained are compared with estimates based separately on the reaction steady state and stationary state assumptions. Results are discussed in terms of the enzyme/substrate inventory used and it is found that the reaction steady state is a satisfactory approximation only when this ratio is sufficiently small. The stationary state may be a better approximation at other values, particularly when enzyme is added to substrate or when an empty tank is being filled. Reaction yields from semi-batch and batch operations are compared. Processing takes longer in the semi-batch operations and complete conversions are only practical in this mode when enzyme is added to substrate.     

Screen‐printed biosensor for allergens

Allergen levels in indoor environments, leading to many diseases, eg asthma, rhinitis and conjunctivitis, affect a large and increasing fraction of the population. A quite effective and inexpensive method of a rough but very rapid overall assessment of total allergen level in the environment has been developed. The method involved estimation of protein in allergen extracts by screen‐printed electrodes using two different techniques. The biosensor comprised a rhodinised carbon working electrode, a silver/silver chloride reference electrode and a carbon counter electrode. In the first method the enzyme protease reacted with allergen protein to release amino acid, which produced hydrogen peroxide in the presence of amino acid oxidase. This was detected amperometrically. The second method used potassium bromide as electrolyte and the electrode was subjected to dual potential. Bromine, released due to electrolysis at higher potential, was consumed by the allergen protein at lower potential. In the first method, a unique technique was used to microencapsulate the enzyme protease and immobilise it on the surface of the electrode by in‐situ polymerisation to avoid contact with the amino acid oxidase. A total of seven allergens were tested and the results gave a good correlation with the standard protein measurement method. Environmental specimens from indoors, schools and workplaces can be evaluated for the aeroallergens produced by dust mites, animal hairs, cockroach debris, pollens, etc as a means of determining the exposure risk. Copyright © 2005 Society of Chemical Industry     

Influence of residual milk-clotting enzyme and proteolysis on melting properties of soft cheese

In this work, we assessed the influence of coagulant residual activity and primary proteolysis on Cremoso Argentino cheese melting properties. For that purpose, we made Cremoso soft cheeses using different amounts of coagulant, and also obtained samples in which milk-clotting enzyme was inactivated. Primary proteolysis correlated with residual activity of coagulant in early stages of cheese ripening; however, it was similar in all cheeses after 30 days. The hydrolysis of caseins did not significantly affect the melting ability of the cheeses, expressed as the area increase after heating samples under standardized conditions. Samples with similar proximate composition showed some changes in meltability; those seemed related to pH evolution during ripening.     

Bisensors for amino acids

Two kinds of biosensors for amino acids (one with nonspecific enzyme as bioelement, the other with specific enzyme(s) as bioelement), including their principles, applications, recent researches and future trends were discussed in detail. 61 references were given. A part of work for gaining Ph. D in chemical and biochemical application at FPMs (Mons, Belgique) Synopsis of the first author Xia Jinlan, Male, born in 1963, now at Facult’e Polytechnique de Mons, Belgique     

Kinetic behaviour of muscle LDH immobilized in nylon tubing

Immobilization was carried out of the lactate dehydrogenase (LDH) from rabbit muscle (EC 1.1.1.27), cross-linked through the bifunctional reactive glutar-aldehyde on to nylon tubing (1 m long, 53cm² internal surface area). Immobilized LDH inactivation kinetics are of first order (t_1/2 = 3·6 years, k = 5·4,e^?4 day^?1 to 5°C). The smaller effect of pH on activity than in the case of LDH in solution can be explained on the basis of limitation to proton diffusion towards the support. A limiting effect to free external diffusion of the substrate towards and products from the support was also observed, an effect which seems to determine the effective kinetic behaviour of immobilized LDH. The apparent optimum temperature is centred around 40°C, observing a clear inactivation (thermal denaturation) above this temperature. In the temperature range studied (10–40°C), the co-existence was seen of a kinetic control accompanied by another control, involving diffusional transport of substrates and products, on the global activity of the immobilized enzyme. This makes the Arrhenius profiles curvilinear. Both graphic and statistical non-linear regression analysis of the kinetic data—rate, v, versus substrate concentration [S]—carried out under conditions in which the diffusional limitations can be considered negligible (high recirculation flow rate), permitted investigation of the intrinsic kinetic behaviour of immobilized LDH. In this sense, it can be deduced that the rate equation to which these data seem to be fitted is of the polynomial quotient type in [S] of minimum degree 2:2. Although the diffusional limitations have a marked effect on the type of global kinetics shown by immobilized LDH, temperature was not found to affect its v[S] behaviour. The experimental evidence obtained thus indicates that the rate equation in the 10-40°C temperature range continues to be a rational equation of at least degree 2:2 in [S].     

Immobilized α-amylase from Bacillus licheniformis: a potential enzymic time—temperature integrator for thermal processing

Biphasic and nth-order models were tested as to their usefulness to fit experimental inactivation data of Bacillus licheniformis α-amylase, immobilized on glass beads, and were discussed with respect to their suitability to characterize the considered enzymic system as a time—temperature integrator (TTI) to evaluate heat processes. Both isothermal and non-isothermal inactivation experiments were carried out. Model (kinetic) parameters (rate constant k, activation energy E_A and reaction order n) were estimated using a non-linear regression procedure. The results obtained, especially the activation energy of about 293 kJ mole^–1, indicated a potential use of this system as a TTI for heating processes in the temperature range of 96–108°C.