Mechanism of enzymatic dehairing of skins using a bacterial alkaline protease
Mechanism of enzymatic dehairing of skins using a bacterial alkaline protease
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DOI：
10.1016/j.chemosphere.2007.07.084
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发表时间：
2008-01-01
期刊：
影响因子：
8.8
通讯作者：
Puvanakrishnan, R.
中科院分区：
文献类型：
--
作者：
Sivasubramanian, S.;Manohar, B. Murall;Puvanakrishnan, R.
在皮革生产的传统脱毛过程中，动物皮要经过使用石灰和硫化钠的剧烈化学处理。硫化物减少存在于毛发和表皮中的角蛋白中的二硫键，从而使它们与皮肤分离。石灰是一种碱，通过从蛋白聚糖（皮肤结缔组织的原纤维间成分）切割大部分糖胺聚糖，有助于打开胶原纤维结构。目前，作为化学脱毛的替代方案，正在开发使用蛋白酶避免使用石灰和硫化物的酶基脱毛工艺，因为它们具有环境效益。虽然化学和酶法脱毛工艺的目的都是除去非胶原蛋白和蛋白聚糖，以及纤维开松，酶法脱毛工艺的机理与化学脱毛工艺的机理不同。在这项研究中，我们试图详细研究的头发保存酶脱毛过程中的皮肤使用细菌蛋白酶对传统的头发烧伤化学脱毛过程的机制。定量分析表明，胶原蛋白含量保持不受影响，在两种治疗方法，但有一个显着减少蛋白多糖成分从脱毛毛皮酶法相比，硫化石灰工艺。这是进一步证实了组织化学检查的部分脱毛毛皮使用不同的染色剂，以及免疫组织化学研究去除核心蛋白聚糖。HPLC图谱显示，核心蛋白聚糖被细菌蛋白酶广泛降解。这项研究最终证明，蛋白聚糖的蛋白水解降解和随后的蛋白多糖聚集体的去除在酶法脱毛过程中胶原纤维束的开放中起着重要的作用。(C)2007爱思唯尔有限公司保留所有权利。
In the conventional dehairing process of leather manufacture, animal skins are subjected to a drastic chemical treatment using lime and sodium sulfide. Sulfide reduces disulfide bonds in keratin present in hair and epidermis and thereby detaches them from skin. Lime, being an alkali, contributes to opening up of collagen fiber structure by cleaving a major portion of the glycosaminoglycans from proteoglycans, the interfibrillar elements of skin connective tissue. Currently, as an alternative to chemical dehairing, enzyme based dehairing processes using proteases avoiding the use of lime and sulfide are being developed because of their environmental benefits. Though both chemical as well as enzymatic dehairing processes are aimed at removing noncollagenous proteins and proteoglycans in addition to fiber opening, the mechanism of enzymatic process is distinct from that of the chemical process. In this study, we attempt to study in detail the mechanism of hair saving enzymatic dehairing process for skins using a bacterial protease against the customary hair burn chemical dehairing process. Quantitative analysis shows that the collagen content remains unaffected in both treatments but there is a marked reduction of proteoglycan constituents from dehaired pelts in the enzymatic process when compared to lime-sulfide process. This is further substantiated by histochemical examination of the sections of dehaired pelts using different stains as well as immunohistochemical studies on the removal of decorin. HPLC profile shows that decorin is extensively degraded by the bacterial protease. This Study conclusively demonstrates that proteolytic degradation of decorin and subsequent removal of proteoglycan aggregates play an important role in the opening up of the collagen fiber bundles during enzymatic dehairing. (C) 2007 Elsevier Ltd. All rights reserved.